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[1]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126;
DOI=10.1038/37052; PubMed=9389475 [NCBI, ExPASy, EBI, Israel, Japan]
Klenk H.-P.,
Clayton R.A.,
Tomb J.-F.,
White O.,
Nelson K.E.,
Ketchum K.A.,
Dodson R.J.,
Gwinn M.L.,
Hickey E.K.,
Peterson J.D.,
Richardson D.L.,
Kerlavage A.R.,
Graham D.E.,
Kyrpides N.C.,
Fleischmann R.D.,
Quackenbush J.,
Lee N.H.,
Sutton G.G.,
Gill S.R., ![]()
Kirkness E.F.,
Dougherty B.A.,
McKenney K.,
Adams M.D.,
Loftus B.J.,
Peterson S.N.,
Reich C.I.,
McNeil L.K.,
Badger J.H.,
Glodek A.,
Zhou L.,
Overbeek R.,
Gocayne J.D.,
Weidman J.F.,
McDonald L.A.,
Utterback T.R.,
Cotton M.D.,
Spriggs T.,
Artiach P.,
Kaine B.P.,
Sykes S.M.,
Sadow P.W.,
D'Andrea K.P.,
Bowman C.,
Fujii C.,
Garland S.A.,
Mason T.M.,
Olsen G.J.,
Fraser C.M.,
Smith H.O.,
Woese C.R.,
Venter J.C.;
"The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.";
Nature 390:364-370(1997).
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- FUNCTION: Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing autotrophic growth from CO(2) (By similarity).
- CATALYTIC ACTIVITY: CO + H2O + A = CO2 + AH2.
- COFACTOR: Binds 7 4Fe-4S clusters per heterotetramer (Potential).
- COFACTOR: Binds 2 nickel-iron-sulfur clusters per heterotetramer (Potential).
- SUBUNIT: Heterotetramer of two alpha and two epsilon chains. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta chains with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8) (Potential).
- DOMAIN: Cluster B is an all-cysteinyl-liganded 4Fe4S cluster; cluster C is a mixed Ni-Fe-S cluster which appears to be the active site of CO oxidation. Cluster D is also an all-cysteinyl-liganded 4Fe4S cluster that bridges the two subunits of the CODH dimer. May contain two additional 4Fe-4S clusters, dubbed E and F, that might reroute electron transfer along different paths.
- SIMILARITY: Belongs to the Ni-containing carbon monoxide dehydrogenase family.
- SIMILARITY: Contains 2 4Fe-4S ferredoxin-type domains.
- CAUTION: This protein lacks the conserved Cys in positions 65 and 69; they are replaced by a Gln and an Asn, respectively. It is therefore possible that the C- and D-clusters are either altered or missing in this protein, which may not form heterotetramers.
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Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
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| Length: 802 AA [This is the length of the unprocessed precursor] |
Molecular weight: 89524 Da [This is the MW of the unprocessed precursor] |
CRC64: 81C626EDED06F66C [This is a checksum on the sequence] |
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10 20 30 40 50 60
MFELKKGALF VDEMKNVSIR IGKVVEEEEE VWEEAGPTPK PGILELRKWD HKLLERYEPF
70 80 90 100 110 120
YAPMQDFCNL CTMGPCDLSM NKRGACGIDL KTAKARLVTI ACCIGASAHT AHARHLVDHL
130 140 150 160 170 180
IEEFGEDFPI DLGGDVNVEA PIIRTVVGIK PKTLGDLREA LNWAEKEIVK VLHSTHIGNE
190 200 210 220 230 240
ESLLDYESKA MHVSMADHVG MEVADIAQIV AYNFPKAEPD TPLVDTGFGI VDKSKPTIVV
250 260 270 280 290 300
VGHNVMYARP VADYLEEMGR IDDFELAGLC CTAHDMTRYN AKAKIFGPIS YQLRVIRAGI
310 320 330 340 350 360
PDVMISDEQC IRADLLEACK KMGIPLIATS DAAARGLPDV SDWPVEKIVD ALVSGKLPGV
370 380 390 400 410 420
FLPIPEKVGQ VAPLVAEAIF KKHGGERKYK FFESDEALME EINKCTQCMN CVFTCPHSLR
430 440 450 460 470 480
VDQGMAHAQK TGDLSKLAQL EEQCLACMKC EQACPKNIKI INVIMRANYD RLYNKTGKTR
490 500 510 520 530 540
VGRGPIQDTE IRKVGQPIVF GQIPGVIAAV GCINFPDEMK SIREILEEFL KRRYIVVTSG
550 560 570 580 590 600
CHAMDIGMIK DEEGKTLYEK YPGNFDAGGL VNTGSCVANS HIAGAAIKIA NIFAMRPLRG
610 620 630 640 650 660
NYAEIADYVL NRVGAVGFSW GPYSHKAASI ATGFNRLGVP VVVGPHGTKY RRAYIGKPWK
670 680 690 700 710 720
KDKWWVYDIK SRQKVFIEPA PDSLLVAVET KEEAIVQLAR LCIRPNDTNQ GRQIKLTHYI
730 740 750 760 770 780
ELHQKYYGDL PDDWAVYVRS EADLPLKMRD QLLKVLEEQY GWKIDWDKKK IVEGPVRHFD
790 800
AGFNPTIVEE VYEKYAGEKA PR
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O29165 in FASTA format |
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