ID I0AGY5_IGNAJ Unreviewed; 661 AA.
AC I0AGY5;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Hydrogenase subunit HydB {ECO:0000313|EMBL:AFH48242.1};
GN Name=hydB {ECO:0000313|EMBL:AFH48242.1};
GN OrderedLocusNames=IALB_0530 {ECO:0000313|EMBL:AFH48242.1};
OS Ignavibacterium album (strain DSM 19864 / JCM 16511 / NBRC 101810 /
OS Mat9-16).
OC Bacteria; Ignavibacteriota; Ignavibacteria; Ignavibacteriales;
OC Ignavibacteriaceae; Ignavibacterium.
OX NCBI_TaxID=945713 {ECO:0000313|EMBL:AFH48242.1, ECO:0000313|Proteomes:UP000007394};
RN [1] {ECO:0000313|EMBL:AFH48242.1, ECO:0000313|Proteomes:UP000007394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19864 / JCM 16511 / NBRC 101810 / Mat9-16
RC {ECO:0000313|Proteomes:UP000007394};
RX PubMed=22661972; DOI=10.3389/fmicb.2012.00185;
RA Liu Z., Frigaard N.-U., Vogl K., Iino T., Ohkuma M., Overmann J.,
RA Bryant D.A.;
RT "Complete genome of Ignavibacterium album, a metabolically versatile,
RT flagellated, facultative anaerobe from the phylum Chlorobi.";
RL Front. Microbiol. 3:185-185(2012).
CC -!- SIMILARITY: Belongs to the complex I 51 kDa subunit family.
CC {ECO:0000256|ARBA:ARBA00007523}.
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DR EMBL; CP003418; AFH48242.1; -; Genomic_DNA.
DR RefSeq; WP_014559400.1; NC_017464.1.
DR AlphaFoldDB; I0AGY5; -.
DR STRING; 945713.IALB_0530; -.
DR GeneID; 78242268; -.
DR KEGG; ial:IALB_0530; -.
DR PATRIC; fig|945713.3.peg.530; -.
DR eggNOG; COG1894; Bacteria.
DR eggNOG; COG3411; Bacteria.
DR HOGENOM; CLU_014881_3_2_10; -.
DR OrthoDB; 9761899at2; -.
DR Proteomes; UP000007394; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR CDD; cd02980; TRX_Fd_family; 1.
DR Gene3D; 3.10.20.600; -; 1.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 6.10.250.1450; -; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR Gene3D; 3.40.50.11540; NADH-ubiquinone oxidoreductase 51kDa subunit; 1.
DR Gene3D; 1.20.1440.230; NADH-ubiquinone oxidoreductase 51kDa subunit, iron-sulphur binding domain; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR001949; NADH-UbQ_OxRdtase_51kDa_CS.
DR InterPro; IPR011538; Nuo51_FMN-bd.
DR InterPro; IPR037225; Nuo51_FMN-bd_sf.
DR InterPro; IPR019575; Nuop51_4Fe4S-bd.
DR InterPro; IPR037207; Nuop51_4Fe4S-bd_sf.
DR InterPro; IPR019554; Soluble_ligand-bd.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR NCBIfam; NF040902; NuoF_pre_CCxxC; 1.
DR PANTHER; PTHR43578; NADH-QUINONE OXIDOREDUCTASE SUBUNIT F; 1.
DR PANTHER; PTHR43578:SF3; NADH-QUINONE OXIDOREDUCTASE SUBUNIT F; 1.
DR Pfam; PF01512; Complex1_51K; 1.
DR Pfam; PF13187; Fer4_9; 1.
DR Pfam; PF10589; NADH_4Fe-4S; 1.
DR Pfam; PF10531; SLBB; 1.
DR SMART; SM00928; NADH_4Fe-4S; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF142019; Nqo1 FMN-binding domain-like; 1.
DR SUPFAM; SSF142984; Nqo1 middle domain-like; 1.
DR SUPFAM; SSF140490; Nqo1C-terminal domain-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
DR PROSITE; PS00645; COMPLEX1_51K_2; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000007394};
KW Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT DOMAIN 604..633
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 634..661
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 661 AA; 72997 MW; 8B8907280F2EEA0E CRC64;
MKNFDQLCCE KCWHTPQNPC EHFIQCCTEG PLCHNDEKCR IEISSLRKRL RYEEHELPII
IIGMGTCGLA SGAGKVKETI LEELKKLNIE AIVESTGCIG YCAVEPIVDV KLPGEDRVSY
CEIVPKIVPK FLHTVLIEKK IFKEKLLGTH GKTNQDARNI NEIPFFEFQR KIVLSNCGII
NPDSIDTYLA YGGFKAFDKV VRLMKPEEVI KEISISGLRG RGGGGFPTGK KWELAYKQKA
DQKYLICNAD EGDPGAFMDR SLLESDPFRV IEGMMIAAYA IGASQAYIYC RAEYPLAIEK
LQNAINLCER YGILGNNILN TGFSLHIKIK KGAGAFVCGE ETALIASIEG KRGMPRPRPP
YPVQAGLWGK PTVINNVETF GNVPSIILMG GEEFAKIGTE KSKGTKVFAL SGNVKNTGLV
EVPMGTTLAD VVFKIGGGIP NGKEFKAVQI GGPSGGCIPE HLIDTPVDYE SLKEIGAMMG
SGGFVVMDED TCMVDVAKYF LTFIQQESCG KCVPCREGTK RMLEIIERIP QRYSSGKDKN
EQLLRFKGMI HLQRLADVIK DTSLCGLGQS APNPVLSGLR YFREEYEEHL YDRKCSAGVC
KELLTFTIDN EKCTGCGICL RKCAVEAIVG EKGQAHYILD EKCIKCGMCV ENCRFDAINV
N
//
