ID   A0A0Q6FA63_9ACTN        Unreviewed;       834 AA.
AC   A0A0Q6FA63;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Carbon monoxide dehydrogenase {ECO:0000313|EMBL:KQT91464.1};
GN   ORFNames=ASG49_10555 {ECO:0000313|EMBL:KQT91464.1};
OS   Marmoricola sp. Leaf446.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Marmoricola.
OX   NCBI_TaxID=1736379 {ECO:0000313|EMBL:KQT91464.1, ECO:0000313|Proteomes:UP000051542};
RN   [1] {ECO:0000313|EMBL:KQT91464.1, ECO:0000313|Proteomes:UP000051542}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf446 {ECO:0000313|EMBL:KQT91464.1,
RC   ECO:0000313|Proteomes:UP000051542};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQT91464.1, ECO:0000313|Proteomes:UP000051542}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf446 {ECO:0000313|EMBL:KQT91464.1,
RC   ECO:0000313|Proteomes:UP000051542};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KQT91464.1}.
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DR   EMBL; LMRF01000003; KQT91464.1; -; Genomic_DNA.
DR   RefSeq; WP_056541426.1; NZ_LMRF01000003.1.
DR   AlphaFoldDB; A0A0Q6FA63; -.
DR   STRING; 1736379.ASG49_10555; -.
DR   OrthoDB; 9758509at2; -.
DR   Proteomes; UP000051542; Unassembled WGS sequence.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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; 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   PANTHER; PTHR11908:SF164; DEHYDROGENASE, MOLYBDENUM BINDING SUBUNIT-RELATED; 1.
DR   PANTHER; PTHR11908; XANTHINE DEHYDROGENASE; 1.
DR   Pfam; PF01315; Ald_Xan_dh_C; 1.
DR   Pfam; PF02738; MoCoBD_1; 1.
DR   Pfam; PF20256; MoCoBD_2; 1.
DR   SMART; SM01008; Ald_Xan_dh_C; 1.
DR   SUPFAM; SSF54665; CO dehydrogenase molybdoprotein N-domain-like; 1.
DR   SUPFAM; SSF56003; Molybdenum cofactor-binding domain; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000051542}.
FT   DOMAIN          30..145
FT                   /note="Aldehyde oxidase/xanthine dehydrogenase a/b
FT                   hammerhead"
FT                   /evidence="ECO:0000259|SMART:SM01008"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          808..834
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        820..834
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   834 AA;  89205 MW;  AE223F9807BEDAF2 CRC64;
     MTATQDAPTT EPRLEIGRDR RRKEDQRLIT GRTKWTDNIQ INGMLHLAMV RSPFAHAKIT
     NIDVSEAKAS RNVVDVLTGA DLAETQGVLI NAWPITPDQV TPTHLPVPAD RVSFAGEIVA
     VVVARSQAEA RDAAELVDVD YEELPAALDL KEAAADTVLA HPDLGTNKSA LWKFDSAEAG
     TGGDVEEAIS KAREGGVVIE REFRQQRLIP AFMEPRSTVV DPTGEQLTMW SATQIPHILR
     FALAATTGMP ESKIRVIAPD VGGGFGGKLQ TTPEEWITVA VARRTGKPVK FTETRSESLM
     SAHHGRDQWQ KLTLAAEKDG TVTGLKVELL ADLGSYVSLV GGGVPVLGAF MFNAIYKFPA
     YHFACQTVLT NKTWTDAYRG AGRPEATFGI ERIMDELALE LGVDPLEVRE KNWIKAEEFP
     FTTVAGLEYD SGNYEAATAK AKEMFGYDEL RAEQKQRRES GDKVQLGIGV STFTEMCGLA
     PSRVLGSLDY GAGGWEHASV RMLATGKVEI VTGASAHGQG HETAFSQIVA DRLGVPFEDV
     EVLHGDTQVA AKGLDTYGSR SLVVGGEALV KATDKVVEKA KPVAAHLLEA NVEDIEFKAG
     SFGVRGTDAA VSIQDVAGAV FVAHNLPDGM EPSLDSDATY DPINFNYPHG THLCAMEVDT
     ETGQVKMRKY TCVDDIGNVI NPLIVEGQVH GGLVQGIAQA LWEEAVYDDS GTLVSASFVD
     YLVPTAADTI NYDVGHNTTP SLTNTLGTKG VGEAGTIAST PAVVNSVLDA IRQFGVKDIQ
     MPCTPERVWK AIQDGTAGAT EDTVGAAAAH FDPATDGEGQ SQRHDGNSSE GAGQ
//