ID   A0A0A1D177_9MICC        Unreviewed;       505 AA.
AC   A0A0A1D177;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=glycine dehydrogenase (aminomethyl-transferring) {ECO:0000256|ARBA:ARBA00012134};
DE            EC=1.4.4.2 {ECO:0000256|ARBA:ARBA00012134};
GN   ORFNames=ART_3576 {ECO:0000313|EMBL:AIY03175.1};
OS   Arthrobacter sp. PAMC 25486.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=1494608 {ECO:0000313|EMBL:AIY03175.1, ECO:0000313|Proteomes:UP000030301};
RN   [1] {ECO:0000313|EMBL:AIY03175.1, ECO:0000313|Proteomes:UP000030301}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PAMC25486 {ECO:0000313|EMBL:AIY03175.1,
RC   ECO:0000313|Proteomes:UP000030301};
RA   Jung J.-H., Joe M.-H., Cho Y.-J., Lee S.G., Han S.J., Lim S., Choi J.-I.;
RT   "Complete genome sequence of Arthrobacter sp. PAMC25486 isolated from the
RT   Arctic.";
RL   Submitted (APR-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};
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DR   EMBL; CP007595; AIY03175.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A1D177; -.
DR   STRING; 1494608.ART_3576; -.
DR   KEGG; arm:ART_3576; -.
DR   HOGENOM; CLU_004620_5_0_11; -.
DR   Proteomes; UP000030301; Chromosome.
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:AIY03175.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030301}.
FT   DOMAIN          140..254
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
FT   DOMAIN          332..436
FT                   /note="Glycine dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21478"
FT   REGION          477..505
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   505 AA;  55411 MW;  F85948BD5D919334 CRC64;
     MPVVEAADLQ GTPEQSFRRT AALTLPQIGQ SQVLRHYLRL SQETLGADLN VDIGQGTCTM
     KYSPKANERF VRSPQSVHMH PLQHESTVQG TLQVLSELED YLAEISGMDA VSLQAGSGSA
     AIYGNVKIVQ AYHADRGAGQ VRDEVITTIF SHPSNAATAK TAGYKVITLY PDENGFPDLE
     ALKSVLSERT AALFITNPED TGIFNPRITE YVDAVHAVGG ICVYDQANAN GLLGITRARE
     AGFDLCHFNL HKTFSTPHAC GGPAAGAIGA TAELAPFLPG RRVRPSDTGY TLTAQDDAAT
     ADVRPFHGVI PNLIRAYAWI RSLGPEGLRQ VSEIAVLNNN YLLAEVLKID GISVPYSEGQ
     HRVEQVRYSW SDLTAQTGIT TGEIGARMAD YGFHYWTSHH PYIVPEPVTL EPTESYSKRE
     LDEYIAALRH TAQEARTNPE LLHSAPHRSS IHTVDVDAMT DPDTWATSWR AYRRKYGGEK
     FPAPPRWQAA ADLTQRQRPP KAHHR
//