ID   Q13NN9_PARXL            Unreviewed;       831 AA.
AC   Q13NN9;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   27-MAR-2024, entry version 99.
DE   SubName: Full=Dehydrogenase {ECO:0000313|EMBL:ABE34300.1};
GN   ORFNames=Bxe_B1666 {ECO:0000313|EMBL:ABE34300.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE34300.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE34300.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE34300.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., Lao V.,
RA   Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., Marx C.J.,
RA   Parnell J.J., Ramette A., Richardson P., Seeger M., Smith D., Spilker T.,
RA   Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp genome
RT   shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
CC   -!- SIMILARITY: Belongs to the GcvT family.
CC       {ECO:0000256|ARBA:ARBA00008609}.
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DR   EMBL; CP000271; ABE34300.1; -; Genomic_DNA.
DR   RefSeq; WP_011491637.1; NZ_CP008762.1.
DR   AlphaFoldDB; Q13NN9; -.
DR   STRING; 266265.Bxe_B1666; -.
DR   KEGG; bxb:DR64_6973; -.
DR   KEGG; bxe:Bxe_B1666; -.
DR   PATRIC; fig|266265.5.peg.6078; -.
DR   eggNOG; COG0404; Bacteria.
DR   eggNOG; COG0665; Bacteria.
DR   OrthoDB; 9774591at2; -.
DR   Proteomes; UP000001817; Chromosome 2.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.30.110; Aminomethyltransferase beta-barrel domains; 1.
DR   Gene3D; 3.30.70.1400; Aminomethyltransferase beta-barrel domains; 1.
DR   Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR032503; FAO_M.
DR   InterPro; IPR013977; GCV_T_C.
DR   InterPro; IPR006222; GCV_T_N.
DR   InterPro; IPR029043; GcvT/YgfZ_C.
DR   InterPro; IPR027266; TrmE/GcvT_dom1.
DR   PANTHER; PTHR13847:SF193; PYRUVATE DEHYDROGENASE PHOSPHATASE REGULATORY SUBUNIT, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR13847; SARCOSINE DEHYDROGENASE-RELATED; 1.
DR   Pfam; PF01266; DAO; 1.
DR   Pfam; PF16350; FAO_M; 1.
DR   Pfam; PF01571; GCV_T; 1.
DR   Pfam; PF08669; GCV_T_C; 1.
DR   SUPFAM; SSF101790; Aminomethyltransferase beta-barrel domain; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF103025; Folate-binding domain; 1.
PE   3: Inferred from homology;
FT   DOMAIN          10..380
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          384..438
FT                   /note="FAD dependent oxidoreductase central"
FT                   /evidence="ECO:0000259|Pfam:PF16350"
FT   DOMAIN          440..712
FT                   /note="Aminomethyltransferase folate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01571"
FT   DOMAIN          737..823
FT                   /note="Glycine cleavage T-protein C-terminal barrel"
FT                   /evidence="ECO:0000259|Pfam:PF08669"
SQ   SEQUENCE   831 AA;  90778 MW;  875F66AD7DF989D0 CRC64;
     MSTSIPAHAR VVIIGGGIIG CSVAYHLTRL GWTDVVLLEQ GQLSCGTTWH AAGLVGQLRA
     QESMTRLIRY STALYAELEA DTGLATGWKQ CGSLSVARTA ERMTQLKRTA AVARAYGVAC
     EVIGPQEAGD LWPVMRTDDL LGAVWLPGDG KANPSDLTQA LARGARMRGA RIVENTRVTA
     VHTRTAQDGK ASGAREVSGL AWRNKDGETG TIGADIVVNC AGQWAKAVGR LCGVTVPLHS
     AEHYYIVTER IAGVHPDLPV MRDPDGFIYF KEEVGGLVMG GFEPDAKPWG MNGIPENFEF
     QLLPDDWDQF EILMKNALQR VPALETAQVR QFYNGPESFT PDNNFMLGEA PELRRFFVGA
     GFNSMGIASA GGAGMALAEW IVAGEPTMDL WPVDIRRFAR FNGNDTWLHD RVKETLGLHY
     AMPWPNRELD SARPFRRSPL YSLLRDEGAC FGSKMGWERA NFFAPSPAEA KIDYAFGQQN
     WLPWSGAEHR ACREGVALFD MTSFSKFLVK GRDAQSVLQG IVANDVDVPA GTTVYTGMLN
     ERGGYESDFT LTRLTDDQYL LVTGSAQTTR DFDAIERAIP HDKHCTLVDV TGQYAVLAVM
     GPRSRELLQS VSKADWSNEA FAFGQSREVD LGYATVRATR LTYVGELGWE LYVPVEFAVG
     VYETLHAAGK AFGLVNAGYY AIDSLRIEKG YRAWGRELTP DTNPFEAGLS FACKLDKDIA
     FRGRDALLKL RAQPLRRRMV VLTADGAAQR MLWGGEAILR DGKPVGFVSS AAFGHTLGCP
     VAMGYVNNPD GAADAAYLNS GRYAIDVAGE LLPATVHLKA PYDPRSERVK N
//