ID F5Z9P3_ALTNA Unreviewed; 965 AA.
AC F5Z9P3;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 77.
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 OrderedLocusNames=ambt_02470 {ECO:0000313|EMBL:AEF02048.1};
OS Alteromonas naphthalenivorans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas.
OX NCBI_TaxID=715451 {ECO:0000313|EMBL:AEF02048.1, ECO:0000313|Proteomes:UP000000683};
RN [1] {ECO:0000313|EMBL:AEF02048.1, ECO:0000313|Proteomes:UP000000683}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 17741 / KACC 18427 / KCTC 11700BP / SN2
RC {ECO:0000313|Proteomes:UP000000683};
RX PubMed=21705606; DOI=10.1128/JB.05252-11;
RA Jin H.M., Jeong H., Moon E.J., Math R.K., Lee K., Kim H.J., Jeon C.O.,
RA Oh T.K., Kim J.F.;
RT "Complete genome sequence of the polycyclic aromatic hydrocarbon-degrading
RT bacterium Alteromonas sp. strain SN2.";
RL J. Bacteriol. 193:4292-4293(2011).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002339; AEF02048.1; -; Genomic_DNA.
DR RefSeq; WP_013782990.1; NC_015554.1.
DR AlphaFoldDB; F5Z9P3; -.
DR KEGG; alt:ambt_02470; -.
DR eggNOG; COG0403; Bacteria.
DR eggNOG; COG1003; Bacteria.
DR HOGENOM; CLU_004620_3_2_6; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000000683; 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; 3.90.1150.10; 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 19..441
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 465..739
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 784..905
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 711
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 965 AA; 104477 MW; BA616C29D07907A6 CRC64;
MSNTSPTLAQ LEQKDAFIRR HVGPGEEEIQ QMLSAIDATS LDDLIAQTVP AGIALPEPLK
VGEGATEVDA LAALKTVAGK NVVNRSFIGM GYYDTHVPNV ILRNVLENPG WYTAYTPYQP
EIAQGRLEAI LNFQQLTIDL TGLELASASL LDEGTAAAEA MTLAKRVSKN KKASSYFIAD
DVHPQTHDVV ATRAEMFGFG IITGPASEAA DHDVFGALLQ YPSTTGEVSD ISDIIAAVQA
KKGIVAVAAD LMSLVLLKSP GELGADVALG SAQRFGVPMG YGGPHAAFFA TRDSYKRSLP
GRIIGVSKDT RGRPALRMAL QTREQHIRRE KANSNICTAQ VLLANMASFY AVYHGPKGLK
TIAQRIHRLT SILATGLTKK GAALKHSTYF DTLTVLVDNK DAVLNKGYEH GLNLRADLEG
AVGVSIDETT TREDIATLFN VILGSDHGLS VEALDADVTT QPASAIPENL LRISDILTHE
VFNQYHSETE MLRYIKSLES KDLALNHSMI SLGSCTMKLN ATAEMIPVTW AEFGQIHPFA
PLNQAEGYQE MIAELAEWLI NVTGYDNLSM QPNSGAQGEY AGLLAIQRYH ESRGEGHRNV
CLIPSSAHGT NPASAQMVSL NVVVVKCDNN GNVDLDDLRK KAEEVGDNLS CAMITYPSTH
GVYEETIREM CEIVHQYGGQ VYMDGANMNA QVGITSPGYI GSDVSHLNLH KTFCIPHGGG
GPGMGPIGVK SHLAPFLPNH TVVNIETTGK DCGAVSAAPW GSASILPISY MYIKMMGSAG
LRKATEVAIL NANYVAKALE GHYNVLYKGQ NGRVAHECII DLRPLKEASG VTEVDIAKRL
NDYGFHAPTM SFPVTGTLMI EPTESEAKYE LDRFVNAMIS IRQEVAKVES GEWDATDNPL
HNAPHTLADI CDSDWNRSYD RNLAAYPVPE VHRNKFWPSV NRIDDVFGDR NLICSCPSIE
SYIEG
//
