ID   A0A317JWE4_9ACTN        Unreviewed;       430 AA.
AC   A0A317JWE4;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=glycine dehydrogenase (aminomethyl-transferring) {ECO:0000256|ARBA:ARBA00012134};
DE            EC=1.4.4.2 {ECO:0000256|ARBA:ARBA00012134};
DE   Flags: Fragment;
GN   ORFNames=DLJ46_24790 {ECO:0000313|EMBL:PWU44670.1};
OS   Micromonospora globispora.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=1450148 {ECO:0000313|EMBL:PWU44670.1, ECO:0000313|Proteomes:UP000245683};
RN   [1] {ECO:0000313|Proteomes:UP000245683}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S2904 {ECO:0000313|Proteomes:UP000245683};
RA   Carro L., Aysel V., Cetin D., Igual J.M., Klenk H.-P., Trujillo M.E.,
RA   Sahin N.;
RT   "Micromonospora globispora sp. nov. and Micromonospora rugosa sp. nov.,
RT   isolated from marine sediment.";
RL   Submitted (MAY-2018) 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:PWU44670.1}.
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DR   EMBL; QGSV01000298; PWU44670.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A317JWE4; -.
DR   Proteomes; UP000245683; 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   CDD; cd00613; GDC-P; 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; IPR049315; GDC-P_N.
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; PF02347; GDC-P; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:PWU44670.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245683}.
FT   DOMAIN          8..429
FT                   /note="Glycine cleavage system P-protein N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02347"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         430
FT                   /evidence="ECO:0000313|EMBL:PWU44670.1"
SQ   SEQUENCE   430 AA;  45569 MW;  2530283F2304FB12 CRC64;
     MSAEQFADRH IGPDPDDERR MLETVGYGSV DELMDAAIPE VIRWHGTLDL PAPASEREAI
     AELRALAARN TVAVSMIGLG YHGTHTPAVI RRNVLENPAW YTAYTPYQPE ISQGRLEALL
     NFQTMVTDLT GLATANASML DEGTAAAEAM TLARRASKSK SPVYVVDADT LPQTVAVITS
     RAEPLGIDVR VLDVERDELP GEFFGLHLQY PGASGAVRDH TGPVEAAHAV GALVTVAADL
     LALALLRAPG EIGADIAAGT TQRFGVPMGF GGPHAGYLAV RAGLERMLPG RLVGVSRDAD
     GNPAYRLALQ TREQHIRREK ATSNICTAQV LLAVMAGMYA VYHGPDGLRA IARRTHDMAA
     RLAAGLRAGG VEVVDVAFFD TVTALVPGRA AQVVAAAAER NVNLRLVDGD RVGISCDETT
     TPAHLAAVWA
//