ID A5D4G2_PELTS Unreviewed; 923 AA.
AC A5D4G2;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE SubName: Full=Aerobic-type carbon monoxide dehydrogenase {ECO:0000313|EMBL:BAF58860.1};
GN OrderedLocusNames=PTH_0679 {ECO:0000313|EMBL:BAF58860.1};
OS Pelotomaculum thermopropionicum (strain DSM 13744 / JCM 10971 / SI).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfotomaculaceae;
OC Pelotomaculum.
OX NCBI_TaxID=370438 {ECO:0000313|EMBL:BAF58860.1, ECO:0000313|Proteomes:UP000006556};
RN [1] {ECO:0000313|Proteomes:UP000006556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13744 / JCM 10971 / SI {ECO:0000313|Proteomes:UP000006556};
RX PubMed=18218977; DOI=10.1101/gr.7136508;
RA Kosaka T., Kato S., Shimoyama T., Ishii S., Abe T., Watanabe K.;
RT "The genome of Pelotomaculum thermopropionicum reveals niche-associated
RT evolution in anaerobic microbiota.";
RL Genome Res. 18:442-448(2008).
CC -!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00006849}.
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DR EMBL; AP009389; BAF58860.1; -; Genomic_DNA.
DR AlphaFoldDB; A5D4G2; -.
DR STRING; 370438.PTH_0679; -.
DR KEGG; pth:PTH_0679; -.
DR eggNOG; COG1529; Bacteria.
DR eggNOG; COG2080; Bacteria.
DR HOGENOM; CLU_001681_2_3_9; -.
DR Proteomes; UP000006556; Chromosome.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 1.10.150.120; [2Fe-2S]-binding domain; 1.
DR Gene3D; 3.90.1170.50; Aldehyde oxidase/xanthine dehydrogenase, a/b hammerhead; 1.
DR Gene3D; 3.30.365.10; Aldehyde oxidase/xanthine dehydrogenase, molybdopterin binding domain; 4.
DR InterPro; IPR002888; 2Fe-2S-bd.
DR InterPro; IPR036884; 2Fe-2S-bd_dom_sf.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR000674; Ald_Oxase/Xan_DH_a/b.
DR InterPro; IPR036856; Ald_Oxase/Xan_DH_a/b_sf.
DR InterPro; IPR016208; Ald_Oxase/xanthine_DH-like.
DR InterPro; IPR008274; AldOxase/xan_DH_MoCoBD1.
DR InterPro; IPR046867; AldOxase/xan_DH_MoCoBD2.
DR InterPro; IPR037165; AldOxase/xan_DH_Mopterin-bd_sf.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR PANTHER; PTHR11908:SF132; ALDEHYDE OXIDASE 1-RELATED; 1.
DR PANTHER; PTHR11908; XANTHINE DEHYDROGENASE; 1.
DR Pfam; PF01315; Ald_Xan_dh_C; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF01799; Fer2_2; 1.
DR Pfam; PF02738; MoCoBD_1; 1.
DR Pfam; PF20256; MoCoBD_2; 1.
DR SMART; SM01008; Ald_Xan_dh_C; 1.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF47741; CO dehydrogenase ISP C-domain like; 1.
DR SUPFAM; SSF54665; CO dehydrogenase molybdoprotein N-domain-like; 1.
DR SUPFAM; SSF56003; Molybdenum cofactor-binding domain; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000006556}.
FT DOMAIN 3..80
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 923 AA; 99858 MW; 08E7236A40CAFFD5 CRC64;
MMQKKFLNIN GVAHTLIVDP EASLADVLRG QLRLTGTKIG CGKAQCGACS VIMNGKVIMS
CATKMKRVPD EAIITTIEGI GTPTNLHALQ MAWVKHGAAQ CGFCAPGFIV SAKVLLDQNP
NPTREEVRDW FQKHRNVCRC TGYKPIVDAV MDAARLMRGE ITPEALGFKM PADGKIWGTD
YPRPSAIGKA TGTINYGSDL GLKMPPGTLQ LKLVQAQVSH ARILSIDTSE AEKMPGVYKV
VTHKDVKGKN RITGLITFPT NKGDGWDRPI LCDEKVFQFG DAIAIVCADT EANAQAAVEK
VKVELEVLPP YMSAPAAMAP DAIEIHPGTP NVYFRQNIAK GEDTGPIMEK ADYVVAIEDY
YVGRQPHLPI EPDVAAAYFD EQGRLVIMSK SIGLDLHHAM IAPGLGIEPE KLILAQFPAV
GGTFGYKFSP TIEALVGAAA MATGKPVFLN FNYFQQITYT GKRSPFFIDL KYGANKDGKI
IAMESNWAVD HGPYSEFGDL LTLRGAQFIG AGYGIPNIRG AGYTVCTNHA WGSAFRAYGS
PQSFFASESL MDILAEKMGI DPLELRYRNV YRPGDTSPTG QPPEVYTLPQ MIDILRPKYK
AALEEARRLS TPEKKRGVGV SIGIYGCGLD GPDSAEVWVE LLPDGRVQVS TNWQDHGQGA
DMGLLATSHE SLRPMGIKPE QIKLVMNDMA VAPAGGPAGG SRSQFVIGNA VKNGCEQLLN
AMRKPDGTYR TYEEMVRENI PLKYVGKWTT PCTPCDENAQ GSPFASYMYG VFMAEVEVDT
RTGKVQVLKM TLVADIGKIA NKTVVDGQIY GGLAQGIGLA LTEDFEDLNK HTTMAACGIP
YIKDVPDNLE VIYVDSPREL GPHGASGVGE LPLTSPHAAI ANAIYNACGV RITQLPALPE
KILAGLQGKQ IPVVRRPIKN PPF
//
