ID A0A117SEG3_9FIRM Unreviewed; 1151 AA.
AC A0A117SEG3;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Hydrogenase {ECO:0000313|EMBL:KUO66976.1};
GN ORFNames=APF84_17440 {ECO:0000313|EMBL:KUO66976.1};
OS Gracilibacter sp. BRH_c7a.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Gracilibacteraceae;
OC Gracilibacter.
OX NCBI_TaxID=1734398 {ECO:0000313|EMBL:KUO66976.1, ECO:0000313|Proteomes:UP000053404};
RN [1] {ECO:0000313|EMBL:KUO66976.1, ECO:0000313|Proteomes:UP000053404}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRH_c7a {ECO:0000313|EMBL:KUO66976.1};
RA Bagnoud A., Chourey K., Hettich R.L., De Bruijn I., Andersson A.F.,
RA Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT "Microbial metabolic network in the subsurface.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KUO66976.1}.
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DR EMBL; LOEZ01000007; KUO66976.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A117SEG3; -.
DR STRING; 1734398.APF84_17440; -.
DR Proteomes; UP000053404; Unassembled WGS sequence.
DR GO; GO:0008901; F:ferredoxin hydrogenase activity; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 3.40.50.1780; -; 1.
DR Gene3D; 3.10.20.440; 2Fe-2S iron-sulphur cluster binding domain, sarcosine oxidase, alpha subunit, N-terminal domain; 1.
DR Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 4.10.260.20; Iron hydrogenase, small subunit; 1.
DR InterPro; IPR042204; 2Fe-2S-bd_N.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR028261; DPD_II.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR009016; Fe_hydrogenase.
DR InterPro; IPR004108; Fe_hydrogenase_lsu_C.
DR InterPro; IPR003149; Fe_hydrogenase_ssu.
DR InterPro; IPR036991; Fe_hydrogenase_ssu_sf.
DR InterPro; IPR013352; Fe_hydrogenase_subset.
DR InterPro; IPR009051; Helical_ferredxn.
DR NCBIfam; TIGR02512; FeFe_hydrog_A; 1.
DR PANTHER; PTHR43073; DIHYDROPYRIMIDINE DEHYDROGENASE [NADP(+)]; 1.
DR PANTHER; PTHR43073:SF2; DIHYDROPYRIMIDINE DEHYDROGENASE [NADP(+)]; 1.
DR Pfam; PF02906; Fe_hyd_lg_C; 1.
DR Pfam; PF02256; Fe_hyd_SSU; 1.
DR Pfam; PF13510; Fer2_4; 1.
DR Pfam; PF14691; Fer4_20; 1.
DR Pfam; PF12838; Fer4_7; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00419; ADXRDTASE.
DR SMART; SM00902; Fe_hyd_SSU; 1.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR SUPFAM; SSF53920; Fe-only hydrogenase; 1.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 4: Predicted;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 8..89
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 620..650
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 663..692
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 1151 AA; 127821 MW; 1B15AB9A8372F951 CRC64;
MKKITKHNRI TVTVNGREME VYDDLTILQA LIQEDIHIPH LCYDIRLERS NGNCGLCVVE
LGEGHDQRDV KACHTPIKEG MVICTNSPKL ENYRKIRLEQ ILSDHNADCV APCVMTCPAN
IDIQAYLRHA GNGNFEAAVQ VIKEKNPFPI VCGRVCPHPC EAQCRRNLID SPVAINNVKR
FIADWDIERE QPWIPKKNPA TGKKIAVVGA GPSGLTASYY SAINGHDVTV FEGQSYAGGM
MRYGIPEYRL PEATLDQEIE LIKSLGVKIM TKKKLGTHIH LEDLHKDFDA VYLGIGSWRA
TSLQIEGENL EGVWLGIQFL EQVTKQEEIK LGNNVIVIGG GNTAIDCART ALRKGAKSVK
LVYRRTMEDM PAEAYEVEEA LQEGVEMLFL TAPSKIVAEG GKKVLHCIQM ELGEPDRSGR
RRPIPIEGSD IHVEADTIIG AIGQSTNTQF LYNDLPVKLN KWGDIEINGK TSQTSELNIF
AGGDCVTGPA TVIQAVAAGR RAAEAMDSFL MKGYVKEQHI DYSCSRGSME DLPKWEFEII
PKLERAKMPA ISIEERKNNF KEVDLGYTEQ TAREEARRCL KCGCHERYDC DLRNEASAHN
IEYSNPTHER PLIPLVEDHS VIVRDHNKCI SCGRCIAACA EVEGPDVLTF YMKHGRQLVG
TKSGLPLEKT DCVSCGQCVN ACPCGALDYR SEKGKVFRAI NDPDKTVVAF VAPAVRSVVS
SHFGIPFNDA SSFMAGLLKK MGFNKVFDFT FAADLTIIEE TTEFLNRIAK EEVMPQFTSC
CPGWVNFVER RYPEIIPHLS SCKSPQMMMG ATVKNHFTKL EGIDKKDLYV VSIVPCIAKK
YEAARPEFAP EGMRDVDAVL TSTEMLEMVE QKLIDPNDVV PQDFCNPYKR VSGAGILFGA
SGGVAEAALR MAVEKLTGKV LTDHLDFEEV RGFEGVKEAT VEASGTKVHV AVISGLNNAE
PIIEKIIQGV DVGYDLIEVM ACPGGCICGA GHPVPEKIDA LEKRQQVLVD IDKTSIYRKS
QENPDVLRLY KDFYGEANSD LAHKLLHTQY SPVNSEYVGI NVRKKDDSAF VTREFTICTC
DACTALGSKE LYHKMTDKIE QLKMNAFVRV KTIRLKGNHT GSGKQIYITL DGKIIEEPKF
EDIYKSIHQP I
//