ID I0ANF9_IGNAJ Unreviewed; 1078 AA.
AC I0ANF9;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Anaerobic dehydrogenase {ECO:0000313|EMBL:AFH50516.1};
GN OrderedLocusNames=IALB_2813 {ECO:0000313|EMBL:AFH50516.1};
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:AFH50516.1, ECO:0000313|Proteomes:UP000007394};
RN [1] {ECO:0000313|EMBL:AFH50516.1, 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 prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR EMBL; CP003418; AFH50516.1; -; Genomic_DNA.
DR RefSeq; WP_014561655.1; NC_017464.1.
DR AlphaFoldDB; I0ANF9; -.
DR STRING; 945713.IALB_2813; -.
DR GeneID; 78244364; -.
DR KEGG; ial:IALB_2813; -.
DR PATRIC; fig|945713.3.peg.2833; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_008235_0_0_10; -.
DR OrthoDB; 9792592at2; -.
DR Proteomes; UP000007394; Chromosome.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd02780; MopB_CT_Tetrathionate_Arsenate-R; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.30.200.210; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR037946; MopB_CT_Tetrathionate.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR43742:SF9; TETRATHIONATE REDUCTASE SUBUNIT A; 1.
DR PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000007394};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 58..131
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 1078 AA; 121046 MW; 8C9DD884238CB14F CRC64;
MKQELIDKSR RSFLAKGALL GGGALAAIFG GEKASAQTQQ LIIKSKRPDV DYPFNKPENI
IYSVCLNCNT GCGIKAKIQD GVLAKIDGNP YNPWTMVPHL SMKTDIDEAA RIDGGLCPKG
QAGVQIAYDP YRIRKVLKRA GKRGENKWIT IPFEQAIQEI VEGGKLFANV PGEENRVVEG
LKDIMALRDA DVAKAMAEDI KAIWDEKDKA KKQELVKAFK EKHKDNLDKL IDPEHPDLGA
KNNQFVMAFG RLKNGRKEFF SRFQSAFGTT NLHGHTTVCQ GSLYFTCKAI SEQYQGGKFT
GGQKFYWQAD LEHAKYVLFV GANLFEANYG PTNRTVRLTE NLAKGYTKIA VADPRFSKLA
SKAHKWLPIK PGTDSALALA MIQWIINNNR YDEKFLRNAN KAAANETNET SWTNANWLVE
IKDGEPGKLI RAADFGLKSA EKRKIEDPKD KTKEIEYEEK FMVVMVNGKP TWVDPNDEKN
PVYGDLFVDT ELTNKEGKKV RVKSGLQILK ESSEENSITK WCEIAGVNEK DVIEVARELT
SYGKQAAVDI HRGPAQHTNG FYNVLSWMSL NMLLGNYDWA GGMCKASTYK YDGSKGGVFD
LTKVKGKIPT FGISSIRHDV DYEKTTIFEG YPAKRNWYPL SSDIYEEIIP SIGDAYPYPV
KALFFYMGAP TYALPAGHTN IDVLADVNKL PLFFCSDIII GSTSMYADYI FPDLSYLERW
EFHGSHPNMP AKVENVRQPV ISPIPEKVKV YGEEIPCSLE AMFMALNEKL GLKAFGKNAL
GDGLDITKPD DFYLRAIANL AYTESPVPDA DERELEVFSK ARRHLDKSVF DEQRWKKVVG
EENWRKVVYI LNRGGRFEDH DKSFDGDKLK HRYAALLNLY QEKTATKKYA ATGKHYYGYA
KYLPIMNYVQ DRVDKISEGY DLHLITHRTI TQTKSRTIAA YWLQPIMPEN GILINPKDAA
KLGIGKDDKV RVISATNIEG KWDFKNGKSK EIVGKAVLTE TMRPGVVSFV LGFGHWATGS
EDFEVDGETI KGDPRRAKGL HANAVMWTDS SLRNNTCMVD PVGGSVSFYD TKVKLVKV
//
