ID A6P0Z8_9FIRM Unreviewed; 908 AA.
AC A6P0Z8;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=Putative selenium-dependent molybdenum hydroxylase 1 {ECO:0000313|EMBL:EDM98019.1};
GN ORFNames=BACCAP_04164 {ECO:0000313|EMBL:EDM98019.1};
OS Pseudoflavonifractor capillosus ATCC 29799.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Pseudoflavonifractor.
OX NCBI_TaxID=411467 {ECO:0000313|EMBL:EDM98019.1, ECO:0000313|Proteomes:UP000003639};
RN [1] {ECO:0000313|EMBL:EDM98019.1, ECO:0000313|Proteomes:UP000003639}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29799 {ECO:0000313|EMBL:EDM98019.1,
RC ECO:0000313|Proteomes:UP000003639};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDM98019.1, ECO:0000313|Proteomes:UP000003639}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29799 {ECO:0000313|EMBL:EDM98019.1,
RC ECO:0000313|Proteomes:UP000003639};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Pseudoflavonifractor capillosus ATCC 29799.";
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00006849}.
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:EDM98019.1}.
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DR EMBL; AAXG02000045; EDM98019.1; -; Genomic_DNA.
DR AlphaFoldDB; A6P0Z8; -.
DR STRING; 411467.BACCAP_04164; -.
DR eggNOG; COG1529; Bacteria.
DR eggNOG; COG2080; Bacteria.
DR OrthoDB; 9759099at2; -.
DR Proteomes; UP000003639; Unassembled WGS sequence.
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:UP000003639}.
FT DOMAIN 13..89
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 908 AA; 97780 MW; 4B5F89984F7A2619 CRC64;
MFLHGWSVDM KEAAIQFVLN GARISCTCDP DMTLLRYLRG TACLKGAKNG CGTGHCGACT
VLMNGRPIRS CITKMSRVDG AEILTIEGLK GEDGGLHPIQ KAFLDVGAIQ CGFCTPGMVL
AAKALLDQNP NPTEQEIVKA LEHNYCRCTG YVKIIEAVAL AAAWLRGEEP SQEEIRFLEH
STISLGEQEA QEPQKYRVLG QSIWDLDGPG KADGTLAYCG DMVRKDMVYG AFVWAPAPKG
RVTGLDLSEA EAMPGVLRVI TAEDVPGENR LGTFDREQPV FCDKEFNFLG DMLALVVAES
EEQARAAAQA VKASWQAADG IYTIEDGIAK GSILMENGRQ TGDVEAARTQ AAVTVSGDYE
LERVEHGCLE PECALGCIED GLLTVYATTQ SPFEIRRMLG HIMAMDESTI KVVGTHLGGG
FGSKCDAHIE AAAAVAAHVM NGPVMINLDR RESLLLSTKR HAYRTSYQVG FNADGTFSYL
DASLCSDAGP YNNLSGGVLM QSCIFAGGPY HIPNISVKGK AVRTNNVLGG AFRGFGINQG
AICIETLMDE AAEKLGLDPF EIRRRNALRI GSRTVGGELL KHSVGLVDTI NLCEKLTREA
VAEYAPLYPR GDKVLGVGVA SGYKNVGVGK GVPDDGGCIL TIREDGKLEM RVSGIDMGQG
FRTAMLQICS EATGWRIEDI DVISGDTSRT LRHGQAVSER QTLNSGRAVV EAAARLKAEC
EANPWQPGER RQAEYYFVAP PTYKLEDEEA RRTQGDEYRN YPAYAYTTQA AIVEVDKSNG
KVKVLKVVAA HDVGRAINPH IIEGQIEGSC SMGIGYALQE SFPSENGVPV NLYYGKLGLP
KAGETPAYEI ALVEDPEPLG PFGAKGISEV ATVPMTPAVL NAIHDAVGVR MRRLPATPER
VLAAMKRR
//
