ID A0A090I624_9GAMM Unreviewed; 955 AA.
AC A0A090I624;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Glycine dehydrogenase (decarboxylating) {ECO:0000256|HAMAP-Rule:MF_00711};
DE EC=1.4.4.2 {ECO:0000256|HAMAP-Rule:MF_00711};
DE AltName: Full=Glycine cleavage system P-protein {ECO:0000256|HAMAP-Rule:MF_00711};
DE AltName: Full=Glycine decarboxylase {ECO:0000256|HAMAP-Rule:MF_00711};
DE AltName: Full=Glycine dehydrogenase (aminomethyl-transferring) {ECO:0000256|HAMAP-Rule:MF_00711};
GN Name=gcvP {ECO:0000256|HAMAP-Rule:MF_00711,
GN ECO:0000313|EMBL:CED57090.1};
GN ORFNames=AWOD_II_0445 {ECO:0000313|EMBL:CED57090.1};
OS Aliivibrio wodanis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Aliivibrio.
OX NCBI_TaxID=80852 {ECO:0000313|EMBL:CED57090.1, ECO:0000313|Proteomes:UP000032427};
RN [1] {ECO:0000313|Proteomes:UP000032427}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=06/09/139 {ECO:0000313|Proteomes:UP000032427};
RA Hjerde E.;
RL Submitted (SEP-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, ECO:0000256|HAMAP-
CC 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;
CC Evidence={ECO:0000256|ARBA:ARBA00043839, ECO:0000256|HAMAP-
CC Rule:MF_00711};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|HAMAP-Rule:MF_00711, ECO:0000256|PIRSR:PIRSR603437-50};
CC -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC T, L and H. {ECO:0000256|ARBA:ARBA00011690, ECO:0000256|HAMAP-
CC Rule:MF_00711}.
CC -!- SIMILARITY: Belongs to the GcvP family. {ECO:0000256|ARBA:ARBA00010756,
CC ECO:0000256|HAMAP-Rule:MF_00711}.
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DR EMBL; LN554847; CED57090.1; -; Genomic_DNA.
DR RefSeq; WP_045103763.1; NZ_LN554847.1.
DR AlphaFoldDB; A0A090I624; -.
DR STRING; 80852.AWOD_II_0445; -.
DR GeneID; 28542695; -.
DR KEGG; awd:AWOD_II_0445; -.
DR PATRIC; fig|80852.17.peg.3207; -.
DR HOGENOM; CLU_004620_3_2_6; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000032427; Chromosome 2 complete sequence.
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 {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00711};
KW Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_00711,
KW ECO:0000256|PIRSR:PIRSR603437-50}.
FT DOMAIN 16..438
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 459..733
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 775..896
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 705
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 955 AA; 104384 MW; 10AAD4DE4A51BFBF CRC64;
MSQLLQQLGT DNEFIRRHNG PASSQHQHML NTVGAETLEK LIEETVPSSI RLPQPMQLPH
GLSENAMLAE LKQIAQQNTL NTSYIGQGYY NTHTPNVILR NVLENPGWYT AYTPYQPEIS
QGRLEALLNY QQMVMDLTGL DIANASLLDE ATAAAEAMTL CKRGGKSKSN TFFVADDVHP
QTLAVIKTRA EFIGFDVVVD TDSNLDSHDV FGALLQYPGT TGEVKDLSTL IEQAQAKKTL
VVVATDLLAS VLLKPVGEMG ADIAIGSAQR FGVPMGYGGP HAAFMATREK LKRSMPGRII
GVSVDSKGNQ ALRMAMQTRE QHIRREKATS NICTAQALLA NMASFYAVYH GPEGLKTIAR
RVHHFTAIVA KALQSAGFEL THQSFFDTLT VKTEQQTDIL YTKALAASIN LRKFDTELGI
SFDETTTVSD LVALLTVFGV DNAECDTLSN EVGADEFAAI PEACRRTSSF LTHPVFNTHH
SETQMLRYLK KLENKDFSLT HGMIPLGSCT MKLNAVAEML PVTWPEFGGI HPFAPLNQAA
GYTTLSTSLK SMLCEITGYD DFSLQPNSGA SGEYAGLIAI QRYHQSRGEG QRNVCLIPSS
AHGTNPATAS MVSMKVVVVK CDDNGNIDMI DLAEKIAKHQ ENLSSIMITY PSTHGVYEEQ
VREVCDMVHE AGGQVYLDGA NMNAQVGLTS PGFIGSDVSH LNLHKTFCIP HGGGGPGMGP
IGVKSHLAPF LPGHTENGVQ GSDYAVSAAD LGSASILPIS WAYIAMMGEM GLTEATKVAI
LNANYVMERL RPHYPVLYRG TNGRIAHECI IDIRPLKEAT GISEEDIAKR LMDFGFHAPT
MSFPVAGTLM IEPTESEDLA ELDRFCDAMI AIREEMNKVQ QGEWPLDNNP LVNAPHTQVD
LMSNEWDHPY TREVACFPST QAKASKYWPT VNRVDNVFGD RNLICSCPSI ENYEE
//
