ID   GCSP_SHEAM              Reviewed;         962 AA.
AC   A1S965;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Glycine dehydrogenase (decarboxylating) {ECO:0000255|HAMAP-Rule:MF_00711};
DE            EC=1.4.4.2 {ECO:0000255|HAMAP-Rule:MF_00711};
DE   AltName: Full=Glycine cleavage system P-protein {ECO:0000255|HAMAP-Rule:MF_00711};
DE   AltName: Full=Glycine decarboxylase {ECO:0000255|HAMAP-Rule:MF_00711};
DE   AltName: Full=Glycine dehydrogenase (aminomethyl-transferring) {ECO:0000255|HAMAP-Rule:MF_00711};
GN   Name=gcvP {ECO:0000255|HAMAP-Rule:MF_00711}; OrderedLocusNames=Sama_2719;
OS   Shewanella amazonensis (strain ATCC BAA-1098 / SB2B).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=326297;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1098 / SB2B;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Fredrickson J.,
RA   Richardson P.;
RT   "Complete sequence of Shewanella amazonensis SB2B.";
RL   Submitted (DEC-2006) 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:0000255|HAMAP-Rule:MF_00711}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-N(6)-lipoyl-L-lysyl-[glycine-cleavage complex H protein] +
CC         glycine + H(+) = (R)-N(6)-(S(8)-aminomethyldihydrolipoyl)-L-lysyl-
CC         [glycine-cleavage complex H protein] + CO2; 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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00711};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00711};
CC   -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC       T, L and H. {ECO:0000255|HAMAP-Rule:MF_00711}.
CC   -!- SIMILARITY: Belongs to the GcvP family. {ECO:0000255|HAMAP-
CC       Rule:MF_00711}.
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DR   EMBL; CP000507; ABM00922.1; -; Genomic_DNA.
DR   RefSeq; WP_011760827.1; NC_008700.1.
DR   AlphaFoldDB; A1S965; -.
DR   SMR; A1S965; -.
DR   STRING; 326297.Sama_2719; -.
DR   EnsemblBacteria; ABM00922; ABM00922; Sama_2719.
DR   KEGG; saz:Sama_2719; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_3_2_6; -.
DR   OMA; CVPMSEY; -.
DR   OrthoDB; 70707at2; -.
DR   Proteomes; UP000009175; Chromosome.
DR   GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IEA:UniProtKB-UniRule.
DR   CDD; cd00613; GDC-P; 2.
DR   Gene3D; 3.40.640.10; -; 2.
DR   Gene3D; 3.90.1150.10; -; 2.
DR   HAMAP; MF_00711; GcvP; 1.
DR   InterPro; IPR003437; GcvP.
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; PTHR11773; 1.
DR   Pfam; PF02347; GDC-P; 2.
DR   SUPFAM; SSF53383; SSF53383; 2.
DR   TIGRFAMs; TIGR00461; gcvP; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..962
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_1000045606"
FT   MOD_RES         709
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   962 AA;  104438 MW;  61179B208FD5969C CRC64;
     MTKQTLTELE QHELFLTRHI GPDADEQQAM LNYVGAESLE DLTAQIVPES IRLGRELNVG
     ASNGEAAGLA YIRQLADKNQ VFKSYIGMGY HGTEVPNVIL RNVLENPGWY TAYTPYQPEI
     AQGRLEAILN FQQLSIDLTG LDLASASLLD EATAAAEAMA LAKRVSKAKK ANTFFVADDV
     FPQTLDVVKT RAECFGFDIV TGPAAEAANH DDLFGALFQY TNRQGQLTDF TELFAQLRAK
     NVIVTVGADI MSLVLLKSPG AMGADVVFGS AQRFGVPMGF GGPHAAFFVS KDEHKRSMPG
     RIIGVSKDTR GKTALRMAMQ TREQHIRREK ANSNICTAQV LLANMASFYA VFHGPQGLKV
     IANRIHRLTD ILAAGLAAKG VTVLNTQWFD TLSFKVDVDA VRARALAAGV NLRYDADGVV
     GVSLAETTTR ADVAELFDII LGAGHGLDVA AIDADILAKG SSSIPAALVR EEAFLTHPTF
     NSYHSETEMM RYIKRLENKD LALNHSMISL GSCTMKLNAA VEMIPVSWPE FANMHPFCPS
     EQAQGYTQLI GELSDWLVDI TGYDAVCMQP NSGAQGEYAG LLAIRKYHES RGEGHRDVCL
     IPQSAHGTNP ASAQLAGMKV VVTACDKQGN VDLDDLRAKA AEVAENLSCI MITYPSTHGV
     YEETVREICD IIHQHGGQVY LDGANMNAQV GLTAPGFIGA DVSHLNLHKT FAIPHGGGGP
     GMGPIGVKKH LAPFVAGHAV VKQGIESDNN GAVSAAPFGS AGILPISWMY IKLLGSKGLK
     QSTQTAMLNA NYLTKKLSEH YPVLYRGRND RIAHECIIDM RPLKEASGVT EMDVAKRLND
     YGFHAPTMSF PVAGTLMIEP TESESKAELD RFIEAMVAIR GEIARVESGE WPVDNNPLAN
     APHTMDDIMD PAFDSRPYSR ELAVFPTESV RANKFWPTVN RIDDVYGDRN LFCACVPMSD
     YE