位置:首页 > 蛋白库 > PHSL_DESBA
PHSL_DESBA
ID   PHSL_DESBA              Reviewed;         514 AA.
AC   P13065;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 3.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Periplasmic [NiFeSe] hydrogenase large subunit;
DE            EC=1.12.99.6;
DE   AltName: Full=NiFeSe hydrogenlyase large chain;
OS   Desulfomicrobium baculatum (Desulfovibrio baculatus).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfomicrobiaceae; Desulfomicrobium.
OX   NCBI_TaxID=899;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3316183; DOI=10.1128/jb.169.12.5401-5407.1987;
RA   Menon N.K., Peck H.D. Jr., le Gall J., Przybyla A.E.;
RT   "Cloning and sequencing of the genes encoding the large and small subunits
RT   of the periplasmic (NiFeSe) hydrogenase of Desulfovibrio baculatus.";
RL   J. Bacteriol. 169:5401-5407(1987).
RN   [2]
RP   ERRATUM OF PUBMED:3316183, AND SEQUENCE REVISION.
RA   Menon N.K., Pect H.D. Jr., le Gall J., Przybyla A.E.;
RL   J. Bacteriol. 170:4429-4429(1988).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS), AND SELENOCYSTEINE AT SEC-493.
RX   PubMed=10378275; DOI=10.1016/s0969-2126(99)80072-0;
RA   Garcin E., Vernede X., Hatchikian E.C., Volbeda A., Frey M.,
RA   Fontecilla-Camps J.-C.;
RT   "The crystal structure of a reduced [NiFeSe] hydrogenase provides an image
RT   of the activated catalytic center.";
RL   Structure 7:557-566(1999).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=A + H2 = AH2; Xref=Rhea:RHEA:12116, ChEBI:CHEBI:13193,
CC         ChEBI:CHEBI:17499, ChEBI:CHEBI:18276; EC=1.12.99.6;
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC       Note=Binds 2 irons ions. Iron 1 has 3 cyanide and carbon monoxide
CC       ligands. Iron 2 has 3 water ligands.;
CC   -!- COFACTOR:
CC       Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC       Note=Binds 1 nickel ion per subunit.;
CC   -!- SUBUNIT: Heterodimer of a large and a small subunit.
CC   -!- SUBCELLULAR LOCATION: Periplasm.
CC   -!- MISCELLANEOUS: Perhaps the leader of the small subunit serves as a
CC       transport vehicle for both subunits.
CC   -!- SIMILARITY: Belongs to the [NiFe]/[NiFeSe] hydrogenase large subunit
CC       family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M18271; AAA23375.2; -; Genomic_DNA.
DR   PIR; A33101; HQDVLB.
DR   PDB; 1CC1; X-ray; 2.15 A; L=2-499.
DR   PDBsum; 1CC1; -.
DR   SMR; P13065; -.
DR   DIP; DIP-6125N; -.
DR   IntAct; P13065; 1.
DR   EvolutionaryTrace; P13065; -.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0008901; F:ferredoxin hydrogenase activity; IEA:InterPro.
DR   GO; GO:0033748; F:hydrogenase (acceptor) activity; IEA:UniProtKB-EC.
DR   GO; GO:0016151; F:nickel cation binding; IEA:InterPro.
DR   Gene3D; 1.10.645.10; -; 1.
DR   InterPro; IPR001501; Ni-dep_hyd_lsu.
DR   InterPro; IPR018194; Ni-dep_hyd_lsu_Ni_BS.
DR   InterPro; IPR029014; NiFe-Hase_large.
DR   Pfam; PF00374; NiFeSe_Hases; 2.
DR   SUPFAM; SSF56762; SSF56762; 1.
DR   PROSITE; PS00507; NI_HGENASE_L_1; 1.
DR   PROSITE; PS00508; NI_HGENASE_L_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Iron; Metal-binding; Nickel; Oxidoreductase; Periplasm;
KW   Selenocysteine.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..514
FT                   /note="Periplasmic [NiFeSe] hydrogenase large subunit"
FT                   /id="PRO_0000199704"
FT   BINDING         52
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT   BINDING         71
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT   BINDING         74
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT   BINDING         74
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT   BINDING         445
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT   BINDING         493
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT   BINDING         496
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT   BINDING         496
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT   BINDING         499
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT   NON_STD         493
FT                   /note="Selenocysteine"
FT   STRAND          14..19
FT                   /evidence="ECO:0007829|PDB:1CC1"
FT   STRAND          22..25
FT                   /evidence="ECO:0007829|PDB:1CC1"
FT   STRAND          27..34
FT                   /evidence="ECO:0007829|PDB:1CC1"
FT   STRAND          37..45
FT                   /evidence="ECO:0007829|PDB:1CC1"
FT   HELIX           51..54
FT                   /evidence="ECO:0007829|PDB:1CC1"
FT   TURN            55..57
FT                   /evidence="ECO:0007829|PDB:1CC1"
FT   HELIX           60..62
FT                   /evidence="ECO:0007829|PDB:1CC1"
FT   HELIX           63..66
FT                   /evidence="ECO:0007829|PDB:1CC1"
FT   HELIX           67..70
FT                   /evidence="ECO:0007829|PDB:1CC1"
FT   STRAND          72..74
FT                   /evidence="ECO:0007829|PDB:1CC1"
FT   HELIX           75..90
FT                   /evidence="ECO:0007829|PDB:1CC1"
FT   HELIX           96..120
FT                   /evidence="ECO:0007829|PDB:1CC1"
FT   HELIX           123..125
FT                   /evidence="ECO:0007829|PDB:1CC1"
FT   HELIX           145..148
FT                   /evidence="ECO:0007829|PDB:1CC1"
FT   HELIX           152..184
FT                   /evidence="ECO:0007829|PDB:1CC1"
FT   STRAND          185..189
FT                   /evidence="ECO:0007829|PDB:1CC1"
FT   STRAND          191..194
FT                   /evidence="ECO:0007829|PDB:1CC1"
FT   STRAND          197..200
FT                   /evidence="ECO:0007829|PDB:1CC1"
FT   HELIX           204..223
FT                   /evidence="ECO:0007829|PDB:1CC1"
FT   HELIX           225..235
FT                   /evidence="ECO:0007829|PDB:1CC1"
FT   HELIX           237..240
FT                   /evidence="ECO:0007829|PDB:1CC1"
FT   STRAND          249..251
FT                   /evidence="ECO:0007829|PDB:1CC1"
FT   STRAND          254..258
FT                   /evidence="ECO:0007829|PDB:1CC1"
FT   STRAND          264..266
FT                   /evidence="ECO:0007829|PDB:1CC1"
FT   STRAND          269..272
FT                   /evidence="ECO:0007829|PDB:1CC1"
FT   STRAND          275..277
FT                   /evidence="ECO:0007829|PDB:1CC1"
FT   HELIX           281..283
FT                   /evidence="ECO:0007829|PDB:1CC1"
FT   STRAND          284..287
FT                   /evidence="ECO:0007829|PDB:1CC1"
FT   STRAND          296..299
FT                   /evidence="ECO:0007829|PDB:1CC1"
FT   HELIX           303..305
FT                   /evidence="ECO:0007829|PDB:1CC1"
FT   STRAND          323..326
FT                   /evidence="ECO:0007829|PDB:1CC1"
FT   HELIX           335..342
FT                   /evidence="ECO:0007829|PDB:1CC1"
FT   HELIX           348..358
FT                   /evidence="ECO:0007829|PDB:1CC1"
FT   HELIX           365..372
FT                   /evidence="ECO:0007829|PDB:1CC1"
FT   HELIX           375..399
FT                   /evidence="ECO:0007829|PDB:1CC1"
FT   STRAND          414..424
FT                   /evidence="ECO:0007829|PDB:1CC1"
FT   STRAND          427..436
FT                   /evidence="ECO:0007829|PDB:1CC1"
FT   STRAND          439..447
FT                   /evidence="ECO:0007829|PDB:1CC1"
FT   HELIX           449..452
FT                   /evidence="ECO:0007829|PDB:1CC1"
FT   HELIX           464..469
FT                   /evidence="ECO:0007829|PDB:1CC1"
FT   HELIX           481..489
FT                   /evidence="ECO:0007829|PDB:1CC1"
FT   HELIX           494..498
FT                   /evidence="ECO:0007829|PDB:1CC1"
SQ   SEQUENCE   514 AA;  56862 MW;  AC920132081C1ADC CRC64;
     MSQAATPAAD GKVKISIDPL TRVEGHLKIE VEVKDGKVVD AKCSGGMFRG FEQILRGRDP
     RDSSQIVQRI CGVCPTAHCT ASVMAQDDAF GVKVTTNGRI TRNLIFGANY LQSHILHFYH
     LAALDYVKGP DVSPFVPRYA NADLLTDRIK DGAKADATNT YGLNQYLKAL EIRRICHEMV
     AMFGGRMPHV QGMVVGGATE IPTADKVAEY AARFKEVQKF VIEEYLPLIY TLGSVYTDLF
     ETGIGWKNVI AFGVFPEDDD YKTFLLKPGV YIDGKDEEFD SKLVKEYVGH SFFDHSAPGG
     LHYSVGETNP NPDKPGAYSF VKAPRYKDKP CEVGPLARMW VQNPELSPVG QKLLKELYGI
     EAKKFRDLGD KAFSIMGRHV LVAEETWLTA VAVEKWLKQV QPGAETYVKS EIPDAAEGTG
     FTEAPRGALL HYLKIKDKKI ENYQIVSATL WNANPRDDMG QRGPIEEALI GVPVPDIKNP
     VNVGRLVRSY DPULGCAVHV LHAETGEEHV VNID
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024