ID A0A162HNL6_9GAMM Unreviewed; 965 AA.
AC A0A162HNL6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
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 ORFNames=A3709_08930 {ECO:0000313|EMBL:KZX55103.1};
OS Halioglobus sp. HI00S01.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae;
OC Halioglobus.
OX NCBI_TaxID=1822214 {ECO:0000313|EMBL:KZX55103.1, ECO:0000313|Proteomes:UP000077184};
RN [1] {ECO:0000313|EMBL:KZX55103.1, ECO:0000313|Proteomes:UP000077184}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HI00S01 {ECO:0000313|EMBL:KZX55103.1,
RC ECO:0000313|Proteomes:UP000077184};
RA Sosa O.A.;
RT "Microbial cycling of marine high molecular weight dissolved organic
RT matter.";
RL Submitted (MAR-2016) 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}.
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:KZX55103.1}.
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DR EMBL; LWEE01000265; KZX55103.1; -; Genomic_DNA.
DR RefSeq; WP_066058346.1; NZ_LWEE01000265.1.
DR AlphaFoldDB; A0A162HNL6; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000077184; Unassembled WGS 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000077184}.
FT DOMAIN 17..442
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 475..736
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 782..903
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 709
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 965 AA; 105098 MW; 90D774399B596995 CRC64;
MSRPSLFELE NHSDFIQRHI GPTVKQQREM AQILGYDSLD ALIDNTVPAA IRRAQPMDLP
GAQTEQNVVR RLKALASQNV INKTFIGTGY HDTFTPPVVQ RNVLENPGWY TAYTPYQPEI
SQGRLEALLS YQQMVMDLTG MDLANASMLD EGTAAAEAMT LLQRVNKKNR SSVFIVAEDC
HPQTIAVIKT RAEVLNIDIV VGNPNELVGK TEAFGVLLQY PGTYGNLDDI APLIEQAHAA
KTLVTVAADI MALLMVKAPG ELGADVVVGN SQRFGVPMGF GGPHAAFFAT RDAYKRSTPG
RIIGVSIDRR GNQALRMAMQ TREQHIRREK ATSNICTAQA LLAIMATFYA MYHGPEGLRT
IASRIHRLTS IFAEGMVGLG FNADNTTYFD TLTFTVCEQQ QAIVHRALAA GMNLRVIGTD
RLGVALDETT TAADIEQLWQ VFSGREDTPD AAALDTGIDG FPGIPAALQR EVDYLQHPLF
NDYHSETEML RYMRYLEDKD IALNRAMIPL GSCTMKLNAT TEMIPVTWPE FAGLHPFAPV
DQTKGYQAML AELDHMLLEA TGYDAISMQP NSGAQGEYAG LLAIMRYHQS RGDHQRNVCL
IPSSAHGTNP ASAALAGMKV VIVECDDNGN IDMADLKTKA ERHTEDLAAI MVTYPSTHGV
FEESIIELCD VVHAHGGQVY VDGANLNALV GIAAPGQFGA DVSHLNLHKT FCIPHGGGGP
GMGPIGVGAH LQPFLPSNPV VPVPGLDENN DVVSAAPYGS ASILPISWSY VALMGGEGLA
QATKVAILNA NYIAHRLKDH YPILYTGTTG NVAHECIIDI RPIKEASGVS EEDIAKRLID
FGFHAPTMSF PVAGTLMVEP TESESMFELD RFCDALIAIK EEINKVQAGE LDAQDNPLAN
APHTLADVAA SEWDHPYSRE LAAYPVASLR RYKYWAPVNR VDNVYGDRNL FCACPAIDSY
REEVE
//
