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Database: UniProt
Entry: A0A097QZ50_HAFAL
LinkDB: A0A097QZ50_HAFAL
Original site: A0A097QZ50_HAFAL 
ID   A0A097QZ50_HAFAL        Unreviewed;       567 AA.
AC   A0A097QZ50;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Hydrogenase 3 large subunit {ECO:0000313|EMBL:AIU71764.1};
GN   Name=hycE {ECO:0000313|EMBL:AIU71764.1};
GN   ORFNames=AT03_04685 {ECO:0000313|EMBL:AIU71764.1};
OS   Hafnia alvei FB1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Hafnia.
OX   NCBI_TaxID=1453496 {ECO:0000313|EMBL:AIU71764.1, ECO:0000313|Proteomes:UP000029986};
RN   [1] {ECO:0000313|EMBL:AIU71764.1, ECO:0000313|Proteomes:UP000029986}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FB1 {ECO:0000313|EMBL:AIU71764.1,
RC   ECO:0000313|Proteomes:UP000029986};
RX   PubMed=25075225; DOI=10.1186/1757-4749-6-29;
RA   Tan J.Y., Yin W.F., Chan K.G.;
RT   "Gene clusters of Hafnia alvei strain FB1 important in survival and
RT   pathogenesis: a draft genome perspective.";
RL   Gut Pathog. 6:29-29(2014).
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|PIRSR:PIRSR601501-1};
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DR   EMBL; CP009706; AIU71764.1; -; Genomic_DNA.
DR   RefSeq; WP_025801577.1; NZ_CP009706.1.
DR   AlphaFoldDB; A0A097QZ50; -.
DR   GeneID; 56890515; -.
DR   KEGG; hav:AT03_04685; -.
DR   PATRIC; fig|1453496.5.peg.937; -.
DR   eggNOG; COG3261; Bacteria.
DR   eggNOG; COG3262; Bacteria.
DR   HOGENOM; CLU_015134_3_1_6; -.
DR   OrthoDB; 9801496at2; -.
DR   Proteomes; UP000029986; Chromosome.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR   GO; GO:0016151; F:nickel cation binding; IEA:InterPro.
DR   GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR   Gene3D; 1.10.645.10; Cytochrome-c3 Hydrogenase, chain B; 1.
DR   Gene3D; 3.30.460.80; NADH:ubiquinone oxidoreductase, 30kDa subunit; 1.
DR   InterPro; IPR001135; NADH_Q_OxRdtase_suD.
DR   InterPro; IPR037232; NADH_quin_OxRdtase_su_C/D-like.
DR   InterPro; IPR001268; NADH_UbQ_OxRdtase_30kDa_su.
DR   InterPro; IPR014029; NADH_UbQ_OxRdtase_49kDa_CS.
DR   InterPro; IPR001501; Ni-dep_hyd_lsu.
DR   InterPro; IPR029014; NiFe-Hase_large.
DR   PANTHER; PTHR43485:SF1; FORMATE HYDROGENLYASE SUBUNIT 5-RELATED; 1.
DR   PANTHER; PTHR43485; HYDROGENASE-4 COMPONENT G; 1.
DR   Pfam; PF00329; Complex1_30kDa; 1.
DR   Pfam; PF00346; Complex1_49kDa; 2.
DR   Pfam; PF00374; NiFeSe_Hases; 1.
DR   SUPFAM; SSF56762; HydB/Nqo4-like; 1.
DR   SUPFAM; SSF143243; Nqo5-like; 1.
DR   PROSITE; PS00535; COMPLEX1_49K; 1.
PE   4: Predicted;
KW   Iron {ECO:0000256|PIRSR:PIRSR601501-1};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR601501-1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR601501-1};
KW   Nickel {ECO:0000256|PIRSR:PIRSR601501-1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029986}.
FT   DOMAIN          35..152
FT                   /note="NADH:ubiquinone oxidoreductase 30kDa subunit"
FT                   /evidence="ECO:0000259|Pfam:PF00329"
FT   DOMAIN          293..462
FT                   /note="NADH-quinone oxidoreductase subunit D"
FT                   /evidence="ECO:0000259|Pfam:PF00346"
FT   DOMAIN          463..535
FT                   /note="NADH-quinone oxidoreductase subunit D"
FT                   /evidence="ECO:0000259|Pfam:PF00346"
FT   BINDING         219
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT   BINDING         239
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT   BINDING         242
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT   BINDING         242
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT   BINDING         529
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT   BINDING         532
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
SQ   SEQUENCE   567 AA;  64533 MW;  4DBA5759A7AC70A5 CRC64;
     MNQQKTGQHY IQELRQQFPS AILDESWQTD TQATITIKTN MLPEVVEFLY YKQGGWLSVL
     FGNDERPLCG SYAVYYVLSM ETGTKCWITV KALVDERTLE FPSVTPRVPA AVWGEREVRD
     MYGLIPVGLP DERRLVLPDD WPDELYPLRK DSMDYRQRPA PTTDVETYPF INESKSGKIV
     PIGPLHITSD EPGHFRLFVD GEDIVDADYR LFYVHRGMEK LAETRMGYNE VTFLSDRVCG
     ICGFAHSTAY TSSVENAMGI QVPERAQAIR SILLEVERLH SHLLNLGLSC HFVGFDSGFM
     QFFRVREKSM KMAEILTGAR KTYGLNLIGG IRRDLLKDDM IQTRKLAAEM RAEVKTLVDI
     LFSTPNMEQR TVGVGRLDPQ IARDFSNVGP MIRASGHARD TRVDHPFAGY DLLPMEIHTE
     TGCDVISRVK VRVNEVFTAL NMIDFGLDNL PGGPLAVEGF TYIPNRFALG FSEAPRGDDI
     HWSMTGDNQK LYRWRCRAAT YSNWPTLRYM LRGNTVSDAP LIIGSLDPCY SCTDRVTLVD
     VRKRKSVTVP YKEIERYGLE RKDSPLK
//
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