ID Q1MR82_LAWIP Unreviewed; 602 AA.
AC Q1MR82;
DT 30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 30-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=Hydrogenase-1 large subunit {ECO:0000313|EMBL:CAJ54494.1};
GN Name=hyaB {ECO:0000313|EMBL:CAJ54494.1};
GN OrderedLocusNames=LI0440 {ECO:0000313|EMBL:CAJ54494.1};
OS Lawsonia intracellularis (strain PHE/MN1-00).
OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC Desulfovibrionaceae; Lawsonia.
OX NCBI_TaxID=363253 {ECO:0000313|EMBL:CAJ54494.1, ECO:0000313|Proteomes:UP000002430};
RN [1] {ECO:0000313|EMBL:CAJ54494.1, ECO:0000313|Proteomes:UP000002430}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHE/MN1-00 {ECO:0000313|EMBL:CAJ54494.1,
RC ECO:0000313|Proteomes:UP000002430};
RA Kaur K., Zhang Q., Beckler D., Munir S., Li L., Kinsley K., Herron L.,
RA Peterson A., May B., Singh S., Gebhart C., Kapur V.;
RT "The complete genome sequence of Lawsonia intracellularis: the causative
RT agent of proliferative enteropathy.";
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000256|PIRSR:PIRSR601501-1};
CC -!- COFACTOR:
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000256|ARBA:ARBA00001967,
CC ECO:0000256|PIRSR:PIRSR601501-1};
CC -!- SIMILARITY: Belongs to the [NiFe]/[NiFeSe] hydrogenase large subunit
CC family. {ECO:0000256|ARBA:ARBA00009292, ECO:0000256|RuleBase:RU003896}.
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DR EMBL; AM180252; CAJ54494.1; -; Genomic_DNA.
DR RefSeq; WP_011526524.1; NC_008011.1.
DR AlphaFoldDB; Q1MR82; -.
DR STRING; 363253.LI0440; -.
DR KEGG; lip:LI0440; -.
DR eggNOG; COG0374; Bacteria.
DR HOGENOM; CLU_030087_0_0_7; -.
DR OrthoDB; 9761717at2; -.
DR Proteomes; UP000002430; Chromosome.
DR GO; GO:0008901; F:ferredoxin hydrogenase activity; IEA:InterPro.
DR GO; GO:0016151; F:nickel cation binding; IEA:InterPro.
DR Gene3D; 1.10.645.10; Cytochrome-c3 Hydrogenase, chain B; 1.
DR InterPro; IPR001501; Ni-dep_hyd_lsu.
DR InterPro; IPR018194; Ni-dep_hyd_lsu_Ni_BS.
DR InterPro; IPR029014; NiFe-Hase_large.
DR PANTHER; PTHR42958:SF3; HYDROGENASE-1 LARGE CHAIN; 1.
DR PANTHER; PTHR42958; HYDROGENASE-2 LARGE CHAIN; 1.
DR Pfam; PF00374; NiFeSe_Hases; 1.
DR SUPFAM; SSF56762; HydB/Nqo4-like; 1.
DR PROSITE; PS00507; NI_HGENASE_L_1; 1.
DR PROSITE; PS00508; NI_HGENASE_L_2; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|PIRSR:PIRSR601501-1};
KW Magnesium {ECO:0000256|PIRSR:PIRSR601501-1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR601501-1};
KW Nickel {ECO:0000256|ARBA:ARBA00022596, ECO:0000256|PIRSR:PIRSR601501-1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003896};
KW Reference proteome {ECO:0000313|Proteomes:UP000002430}.
FT BINDING 57
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 76
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 79
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 79
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 577
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 580
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 583
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
SQ SEQUENCE 602 AA; 67024 MW; F7AA701FF39107A0 CRC64;
MSYQYSTQGY EVTDAGKRIV VDPITRIEGH LRCEVNINSS GIITNAVSSG TLFRGLEIIL
KNRDPRDAWA FAERICGVCT GTHALTSIYA VENALQIEVP ANANFIRNMM QLALWCHDHI
VHFYQLAGLD WIDVVSAAKG DPKKASELAQ SISSWPMSSP GYFADIKKRL VDIIGSGQLG
IFKNGYWGHP AYKLPPEANL MLVAHYIEAL NMQKEVVKIH TIFGGKNPHP NWIVGGMPLA
LNLDAKGGAD VINMERLEYV QRIINICKDF TSKVLMPDTI ALGKFYPEWL SIGKGISHLS
ILSYGGFPTI SNDFSNDSLL VPNGAIINGN FNEVHPVDLF AEDEVREEVS HSWYRYPNDI
TSLHPFEGET IPEFSVGPNT KGTETDIKEL DERARYSWIK TPRWKGHMME VGPLPRVLIA
YYMKREETVT AVDEICRQLN VPVTHMCSTL GRIIARSHEA VWAAEKLQYF FDRLIANTKA
GDLTVANTTK WEPSTWPKEA KGAGFTEAPR GALGHWVVIK DTKIDRYQCV VPTTWNAAPR
SDSEQLGPYE AALMDTHLAE PEKPLELLRT IHSFDPCLAC ATHIIGPDGN EVLSVQCNTA
GC
//
