ID   A0A0W1GRL8_9SPHN        Unreviewed;       530 AA.
AC   A0A0W1GRL8;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=glycine dehydrogenase (aminomethyl-transferring) {ECO:0000256|ARBA:ARBA00012134};
DE            EC=1.4.4.2 {ECO:0000256|ARBA:ARBA00012134};
GN   ORFNames=ATE69_01095 {ECO:0000313|EMBL:KTE57450.1};
OS   Sphingopyxis sp. H071.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingopyxis.
OX   NCBI_TaxID=1759078 {ECO:0000313|EMBL:KTE57450.1, ECO:0000313|Proteomes:UP000054127};
RN   [1] {ECO:0000313|EMBL:KTE57450.1, ECO:0000313|Proteomes:UP000054127}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H071 {ECO:0000313|EMBL:KTE57450.1,
RC   ECO:0000313|Proteomes:UP000054127};
RA   Zhang Y., Guo Z.;
RL   Submitted (NOV-2015) 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:KTE57450.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LNSF01000001; KTE57450.1; -; Genomic_DNA.
DR   RefSeq; WP_058454613.1; NZ_LNSF01000001.1.
DR   AlphaFoldDB; A0A0W1GRL8; -.
DR   OrthoDB; 9801272at2; -.
DR   Proteomes; UP000054127; 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:KTE57450.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898}.
FT   DOMAIN          193..301
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
FT   DOMAIN          382..478
FT                   /note="Glycine dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21478"
SQ   SEQUENCE   530 AA;  56003 MW;  46AFF5A06A231F77 CRC64;
     MTALNRAGWR PEMTAGGADD TVTFTGNRAL MLEEPLIFEI GSSETTGVDF DEETPVADLG
     NLARSTPIGL PGLSESETVR HYTRLSRQNY AIDLGLFPLG SCTMKHNPRL NEKVARMPGF
     ADAHPLQPQE TVQGAYAVIH ELAEWLVTLT GMHSVAMSPK AGAHGELCGI LCIKAALEAR
     GEDRRVLLVP ESAHGTNPAT AAFAGFSVED IPATAEGRVD LAALKARLGP DVAGVMVTNP
     NTCGLFERDM KAISDAVHAA GGYVYCDGAN FNAIVGRVRP GDLGVDAMHI NLHKTFSTPH
     GGGGPGSGPV VLSEALAPFA PLPFVAKQAD GGFRLIEEEN AGEDHPETFG RMTAFHGQMG
     MFTRALTYIL SHGADGLKQV AEDAVLNANY ILRNLEDVLD APFGFSGPCM HEALFSDKGL
     AEGFSTLDVA KGLIDEGYHP MTVYFPLVVH GAMLVEPTET ESKAVLDQFI GALRSIALRA
     KNGDPALKTA PHFAPRARLD ETKAARNPVL AWSEPAAAPG VPVASEVGGG
//