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MBHS_WOLSU
ID   MBHS_WOLSU              Reviewed;         354 AA.
AC   P31884;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=Quinone-reactive Ni/Fe-hydrogenase small chain;
DE            EC=1.12.5.1;
DE   AltName: Full=Hydrogen:quinone oxidoreductase;
DE   AltName: Full=Membrane-bound hydrogenase small subunit;
DE   Flags: Precursor;
GN   Name=hydA; OrderedLocusNames=WS1687;
OS   Wolinella succinogenes (strain ATCC 29543 / DSM 1740 / LMG 7466 / NCTC
OS   11488 / FDC 602W) (Vibrio succinogenes).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Wolinella.
OX   NCBI_TaxID=273121;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 37-52.
RX   PubMed=1587288; DOI=10.1111/j.1432-1033.1992.tb16905.x;
RA   Dross F., Geisler V., Lenger R., Theis F., Krafft T., Fahrenholz F.,
RA   Kojro E., Duchene A., Tripier D., Juvenal K., Kroeger A.;
RT   "The quinone-reactive Ni/Fe-hydrogenase of Wolinella succinogenes.";
RL   Eur. J. Biochem. 206:93-102(1992).
RN   [2]
RP   ERRATUM OF PUBMED:1587288.
RX   PubMed=8319698;
RA   Dross F., Geisler V., Lenger R., Theis F., Krafft T., Fahrenholz F.,
RA   Kojro E., Duchene A., Tripier D., Juvenal K., Kroeger A.;
RL   Eur. J. Biochem. 214:949-950(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29543 / DSM 1740 / CCUG 13145 / JCM 31913 / LMG 7466 / NCTC
RC   11488 / FDC 602W;
RX   PubMed=14500908; DOI=10.1073/pnas.1932838100;
RA   Baar C., Eppinger M., Raddatz G., Simon J., Lanz C., Klimmek O.,
RA   Nandakumar R., Gross R., Rosinus A., Keller H., Jagtap P., Linke B.,
RA   Meyer F., Lederer H., Schuster S.C.;
RT   "Complete genome sequence and analysis of Wolinella succinogenes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:11690-11695(2003).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a menaquinone + H2 = a menaquinol; Xref=Rhea:RHEA:18641,
CC         Rhea:RHEA-COMP:9537, Rhea:RHEA-COMP:9539, ChEBI:CHEBI:16374,
CC         ChEBI:CHEBI:18151, ChEBI:CHEBI:18276; EC=1.12.5.1;
CC   -!- COFACTOR:
CC       Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137; Evidence={ECO:0000250};
CC       Note=Binds 1 [3Fe-4S] cluster. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC       Note=Binds 2 [4Fe-4S] clusters. {ECO:0000250};
CC   -!- SUBUNIT: Heterodimer of a large and a small subunit.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC   -!- PTM: Predicted to be exported by the Tat system. The position of the
CC       signal peptide cleavage has been experimentally proven.
CC   -!- SIMILARITY: Belongs to the [NiFe]/[NiFeSe] hydrogenase small subunit
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA46302.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=CAE10714.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; X65189; CAA46302.1; ALT_INIT; Genomic_DNA.
DR   EMBL; BX571661; CAE10714.1; ALT_INIT; Genomic_DNA.
DR   PIR; S33852; S33852.
DR   AlphaFoldDB; P31884; -.
DR   SMR; P31884; -.
DR   STRING; 273121.WS1687; -.
DR   TCDB; 3.D.7.2.2; the h2:heterodisulfide oxidoreductase (hho) family.
DR   EnsemblBacteria; CAE10714; CAE10714; WS1687.
DR   KEGG; wsu:WS1687; -.
DR   eggNOG; COG1740; Bacteria.
DR   HOGENOM; CLU_046107_0_0_7; -.
DR   Proteomes; UP000000422; Chromosome.
DR   GO; GO:0009375; C:ferredoxin hydrogenase complex; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0008901; F:ferredoxin hydrogenase activity; IEA:InterPro.
DR   GO; GO:0047067; F:hydrogen:quinone oxidoreductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.700; -; 1.
DR   Gene3D; 4.10.480.10; -; 1.
DR   InterPro; IPR027394; Cytochrome-c3_hydrogenase_C.
DR   InterPro; IPR006137; NADH_UbQ_OxRdtase-like_20kDa.
DR   InterPro; IPR037148; NiFe-Hase_small_C_sf.
DR   InterPro; IPR037024; NiFe_Hase_small_N_sf.
DR   InterPro; IPR001821; NiFe_hydrogenase_ssu.
DR   InterPro; IPR006311; TAT_signal.
DR   InterPro; IPR019546; TAT_signal_bac_arc.
DR   PANTHER; PTHR30013; PTHR30013; 1.
DR   Pfam; PF14720; NiFe_hyd_SSU_C; 1.
DR   Pfam; PF01058; Oxidored_q6; 1.
DR   Pfam; PF10518; TAT_signal; 1.
DR   PIRSF; PIRSF000310; NiFe_hyd_ssu; 1.
DR   TIGRFAMs; TIGR00391; hydA; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   1: Evidence at protein level;
KW   3Fe-4S; 4Fe-4S; Cell membrane; Direct protein sequencing; Iron;
KW   Iron-sulfur; Membrane; Metal-binding; Oxidoreductase; Reference proteome;
KW   Signal.
FT   SIGNAL          1..36
FT                   /note="Tat-type signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00648,
FT                   ECO:0000269|PubMed:1587288"
FT   CHAIN           37..354
FT                   /note="Quinone-reactive Ni/Fe-hydrogenase small chain"
FT                   /id="PRO_0000013437"
FT   BINDING         53
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         56
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         153
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         186
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         224
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         227
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         252
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         258
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         267
FT                   /ligand="[3Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21137"
FT                   /evidence="ECO:0000250"
FT   BINDING         286
FT                   /ligand="[3Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21137"
FT                   /evidence="ECO:0000250"
FT   BINDING         289
FT                   /ligand="[3Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21137"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   354 AA;  38294 MW;  C39CC21D2F5AB7D0 CRC64;
     MLEEKGIERR DFMKWAGAMT AMLSLPATFT PLTAKAAELA DRLPVIWLHM AECTGCSESL
     LRTDGPGIDS LIFDYISLEY HETVMAAAGW QAEHNLEHAI EKYKGRYVLM VEGGIPAGSS
     EFYLTVGPHG TTGAEHARHA SANAAAIFAI GSCSSFGGVQ AARPNPTNAQ PLSKVTNKPV
     INVPGCPPSE KNIVGNVLHF ILFGTLPSVD AFNRPMWAYG LRIHDLCERR GRFDAGEFVQ
     EFGDEGAKKG YCLYKVGCKG PYTFNNCSKL RFNQHTSWPV QAGHGCIGCS EPDFWDTMGP
     FEEPVANRLY ATAFDGLGAD KTADKIGITL LAATAVGVAA HAVLSMMVKD KENN
 
 
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