ID   GCSP_VIBC1              Reviewed;         954 AA.
AC   A7N5C4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   27-MAR-2024, entry version 99.
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};
GN   OrderedLocusNames=VIBHAR_05973;
OS   Vibrio campbellii (strain ATCC BAA-1116).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=2902295;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1116 / BB120;
RG   The Vibrio harveyi Genome Sequencing Project;
RA   Bassler B., Clifton S.W., Fulton L., Delehaunty K., Fronick C.,
RA   Harrison M., Markivic C., Fulton R., Tin-Wollam A.-M., Shah N., Pepin K.,
RA   Nash W., Thiruvilangam P., Bhonagiri V., Waters C., Tu K.C., Irgon J.,
RA   Wilson R.K.;
RL   Submitted (AUG-2007) 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=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; 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; CP000790; ABU73866.1; -; Genomic_DNA.
DR   RefSeq; WP_012129510.1; NC_022270.1.
DR   AlphaFoldDB; A7N5C4; -.
DR   SMR; A7N5C4; -.
DR   KEGG; vha:VIBHAR_05973; -.
DR   PATRIC; fig|338187.25.peg.4323; -.
DR   Proteomes; UP000008152; Chromosome II.
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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 2.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 2.
DR   HAMAP; MF_00711; GcvP; 1.
DR   InterPro; IPR003437; GcvP.
DR   InterPro; IPR049316; GDC-P_C.
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   NCBIfam; TIGR00461; gcvP; 1.
DR   PANTHER; PTHR11773:SF13; GLYCINE DEHYDROGENASE (DECARBOXYLATING); 1.
DR   PANTHER; PTHR11773; GLYCINE DEHYDROGENASE, DECARBOXYLATING; 1.
DR   Pfam; PF21478; GcvP2_C; 1.
DR   Pfam; PF02347; GDC-P; 2.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 2.
PE   3: Inferred from homology;
KW   Oxidoreductase; Pyridoxal phosphate.
FT   CHAIN           1..954
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_1000045625"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         704
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   954 AA;  104067 MW;  9FE7A95E6B842F37 CRC64;
     MTELLQSLST QNEFVARHNG PNKSDQQKML EAINAVSLDS LIDETVPAQI RLEQPMNLAE
     AKSEADMLAA MRKFADQNQI KRTFIGQGYY NTFTPNVILR NVMENPGWYT AYTPYQPEIS
     QGRLESLLNY QQMVMDLTGM EIANASLLDE ATAAAEAMTL CKRAGKSKSN VFFVADDVHP
     QTIEVVKTRA KFIGFEVLVG ALDSLPEQDV FGALVQYPGT TGEVRDLTDL IAKAQANKTL
     VTVATDLLAS ALLKPAGEMG ADVAIGSAQR FGVPMGYGGP HAAFMATRDK HKRTMPGRVI
     GVSIDTNGNQ ALRMAMQTRE QHIRREKATS NICTAQALLA NMASFYAVFH GAEGLRTIAR
     RTHHMTAILA AGLTKGGFEL AHNSFFDTIT INTGAQTEDL YAKALAADIN LRKLGTQLGV
     SFDETTTVAD VEALFAVFGV KEEVAALSTE IAGNEFAAIP EALRRTTEYL THPVFNTHHS
     ETQMMRYLKQ LENKDFSLTH GMIPLGSCTM KLNAAAEMIP VTWPEFGSIH PFAPADQAAG
     YAALAKDLKE KLCEITGYDA FSLQPNSGAS GEYAGLIAIQ RYHESRGEGH RNVCLIPSSA
     HGTNPATASM VSMKVVVVKC DEEGNIDVTD LAAKIKKHKD NLSSIMITYP STHGVYEEQV
     KEVCEMVHAA GGQVYLDGAN MNAQVGLTTP GFIGSDVSHL NLHKTFCIPH GGGGPGMGPI
     GVKSHLAPFL PGHIENGADG ENFAVSAADM GSASILPISW AYIAMMGEAG LTDATKVAIL
     NANYVMEQLR PHYPVLYRGS NGRVAHECII DIRPLKEETG ISEEDIAKRL MDYGFHAPTM
     SFPVAGTLMV EPTESEDLEE LDRFCDAMIA IREEMTKVKN GEWPLDNNPL VNAPHTQFDL
     AKEEWDRPYS RELGCFPSKA TKSWKYWPTV NRVDNVYGDR NLICSCPSID NYED
//