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Database: UniProt
Entry: A0A244EI37_9BURK
LinkDB: A0A244EI37_9BURK
Original site: A0A244EI37_9BURK 
ID   A0A244EI37_9BURK        Unreviewed;       531 AA.
AC   A0A244EI37;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Xanthine dehydrogenase small subunit {ECO:0000313|EMBL:OUM04130.1};
GN   ORFNames=A8M77_02965 {ECO:0000313|EMBL:OUM04130.1};
OS   Variovorax sp. JS1663.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=1851577 {ECO:0000313|EMBL:OUM04130.1, ECO:0000313|Proteomes:UP000195166};
RN   [1] {ECO:0000313|EMBL:OUM04130.1, ECO:0000313|Proteomes:UP000195166}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JS1663 {ECO:0000313|EMBL:OUM04130.1};
RX   PubMed=28526789;
RA   Mahan K.M., Zheng H., Fida T.T., Parry R.J., Graham D.E., Spain J.C.;
RT   "A novel, iron-dependent enzyme that catalyzes the initial step in the
RT   biodegradation of N-nitroglycine by Variovorax sp. strain JS1663.";
RL   Appl. Environ. Microbiol. 83:0-0(2017).
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:OUM04130.1}.
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DR   EMBL; LYMK01000002; OUM04130.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A244EI37; -.
DR   OrthoDB; 9179439at2; -.
DR   Proteomes; UP000195166; Unassembled WGS sequence.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004854; F:xanthine dehydrogenase activity; IEA:InterPro.
DR   Gene3D; 3.10.20.30; -; 1.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 1.10.150.120; [2Fe-2S]-binding domain; 1.
DR   Gene3D; 3.30.390.50; CO dehydrogenase flavoprotein, C-terminal domain; 1.
DR   Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR   InterPro; IPR002888; 2Fe-2S-bd.
DR   InterPro; IPR036884; 2Fe-2S-bd_dom_sf.
DR   InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR   InterPro; IPR006058; 2Fe2S_fd_BS.
DR   InterPro; IPR016208; Ald_Oxase/xanthine_DH-like.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   InterPro; IPR005107; CO_DH_flav_C.
DR   InterPro; IPR036683; CO_DH_flav_C_dom_sf.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR002346; Mopterin_DH_FAD-bd.
DR   InterPro; IPR012175; Xanth_DH_ssu_bac.
DR   InterPro; IPR014307; Xanthine_DH_ssu.
DR   NCBIfam; TIGR02963; xanthine_xdhA; 1.
DR   PANTHER; PTHR45444:SF3; ALDEHYDE OXIDASE_XANTHINE DEHYDROGENASE, MOLYBDOPTERIN BINDING PROTEIN; 1.
DR   PANTHER; PTHR45444; XANTHINE DEHYDROGENASE; 1.
DR   Pfam; PF03450; CO_deh_flav_C; 1.
DR   Pfam; PF00941; FAD_binding_5; 1.
DR   Pfam; PF01799; Fer2_2; 1.
DR   PIRSF; PIRSF036557; XdhA_RC; 1.
DR   SMART; SM01092; CO_deh_flav_C; 1.
DR   SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR   SUPFAM; SSF55447; CO dehydrogenase flavoprotein C-terminal domain-like; 1.
DR   SUPFAM; SSF47741; CO dehydrogenase ISP C-domain like; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   PROSITE; PS00197; 2FE2S_FER_1; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   4: Predicted;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022827};
KW   Reference proteome {ECO:0000313|Proteomes:UP000195166}.
FT   DOMAIN          222..395
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   531 AA;  57514 MW;  ED8EE5FEF291DE80 CRC64;
     MSMTPSTQPI RFFHRGRIVD VSGVHPTRSV LDWLREDARC TGTKEGCNEG DCGACTVVIG
     ELAEAGEKGA VGGLRLSTVN ACIQFLPTLH GKALFTVEDL KSQCTRQREK APREKQSTIQ
     LHPVQQALVD CHGSQCGFCT PGFVMSLWST YEHHQDAGTQ PSRQQLADDL SGNLCRCTGY
     RPILDAGQRM FDLPAVRLDT EPVVAALSSL KHEAAFEYAA PLGQRVDHFH APTTLAQLAA
     LREAKPAAQL LSGSTDVGLW VNKQFRDLGD IIYVGDVTEM KVVQERDGEL YIGAGASLEN
     AFSALARRMP SLTDLWLRFA SPPIRNAGTM GGNVANGSPI GDSPPVLMSL DAQIELRLGE
     RVRRMPLSDF YVDYMKNKLA PGEFVQGLAV PLAAMQRQVR AYKISKRFDC DISALCAGFA
     IELDGDTVKE VRLAFGGMAA IVKRGAQAEA ALVGKPWSQA SVNAAKLALA QDFTPLTDMR
     ASADYRLLVA QNLLQRLWLE TRAKDPLPVE ATSVWSVMPH AAAGVVAAEG V
//
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