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Database: UniProt
Entry: A0A013WD76_9SPHN
LinkDB: A0A013WD76_9SPHN
Original site: A0A013WD76_9SPHN 
ID   A0A013WD76_9SPHN        Unreviewed;       522 AA.
AC   A0A013WD76;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=glycine dehydrogenase (aminomethyl-transferring) {ECO:0000256|ARBA:ARBA00012134};
DE            EC=1.4.4.2 {ECO:0000256|ARBA:ARBA00012134};
GN   ORFNames=BF95_24120 {ECO:0000313|EMBL:EXS68161.1};
OS   Sphingobium sp. Ant17.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=1461752 {ECO:0000313|EMBL:EXS68161.1, ECO:0000313|Proteomes:UP000021537};
RN   [1] {ECO:0000313|EMBL:EXS68161.1, ECO:0000313|Proteomes:UP000021537}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ant17 {ECO:0000313|EMBL:EXS68161.1,
RC   ECO:0000313|Proteomes:UP000021537};
RA   Adriaenssens E.M., Cowan D.A.;
RT   "Draft genome sequence of the aromatic hydrocarbon-degrading bacterium
RT   Sphingobium sp. strain Ant17 isolated from Antarctic soil.";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The glycine cleavage system catalyzes the degradation of
CC       glycine. The P protein binds the alpha-amino group of glycine through
CC       its pyridoxal phosphate cofactor; CO(2) is released and the remaining
CC       methylamine moiety is then transferred to the lipoamide cofactor of the
CC       H protein. {ECO:0000256|ARBA:ARBA00003788}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycine + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[glycine-cleavage
CC         complex H protein] = CO2 + N(6)-[(R)-S(8)-aminomethyldihydrolipoyl]-
CC         L-lysyl-[glycine-cleavage complex H protein]; Xref=Rhea:RHEA:24304,
CC         Rhea:RHEA-COMP:10494, Rhea:RHEA-COMP:10495, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:57305, ChEBI:CHEBI:83099,
CC         ChEBI:CHEBI:83143; EC=1.4.4.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00043839};
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:EXS68161.1}.
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DR   EMBL; JEMV01000101; EXS68161.1; -; Genomic_DNA.
DR   RefSeq; WP_043154971.1; NZ_JEMV01000101.1.
DR   AlphaFoldDB; A0A013WD76; -.
DR   STRING; 1461752.BF95_24120; -.
DR   PATRIC; fig|1461752.3.peg.5154; -.
DR   OrthoDB; 9801272at2; -.
DR   Proteomes; UP000021537; Unassembled WGS sequence.
DR   GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006546; P:glycine catabolic process; IEA:InterPro.
DR   Gene3D; 6.20.440.10; -; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR000192; Aminotrans_V_dom.
DR   InterPro; IPR049316; GDC-P_C.
DR   InterPro; IPR020581; GDC_P.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR11773:SF1; GLYCINE DEHYDROGENASE (DECARBOXYLATING), MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11773; GLYCINE DEHYDROGENASE, DECARBOXYLATING; 1.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   Pfam; PF21478; GcvP2_C; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:EXS68161.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898}.
FT   DOMAIN          187..302
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
FT   DOMAIN          382..480
FT                   /note="Glycine dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21478"
SQ   SEQUENCE   522 AA;  55258 MW;  7F8634B49848072C CRC64;
     MTMLKEGRPT TPVAVVDAHM APATATGNRA LMLEEALIFE IGSTETTGVD FAPAPKVASR
     LGGLARKAIG LPGLSEQETV RHYTRLSRQN YAIDLGLFPL GSCTMKHNPR LNEKVARMPG
     FADLHPLAPQ STVQGALAVI HELAAWLVTL TGMHSVAMSP KAGAHGELCG LLAIRAALEA
     RGDARSVVLV PESAHGTNPA TAAFCGYQVE DIPATPEGRV DLAALTARLG PDVAAVMITN
     PNTCGLFERD LKTISDAVHA VGAFVYCDGA NFNAIVGRVR PGDLGVDAMH INLHKTFSTP
     HGGGGPGSGP VVLSAALAPY APLPFVEKQG DQFVLIEEES AQDHHGGTFG RMVAFHGQMG
     MFTRALAYIM SHGADGLRQV AEDAVLNANY ILRSLDDVLD APFGASGPCM HEALFSDKGL
     AEGFTTLDIA KGLIDEGFHP MTMYFPLVVH GAMLIEPTET ESKAALDQFI LALRSLAERA
     KAGDELLKGA PYHAPRRRLD ETLAARKPVL TWEAPVQAQA AE
//
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