ID A0A2S4HC04_9GAMM Unreviewed; 958 AA.
AC A0A2S4HC04;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
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:POP51487.1};
GN ORFNames=C0068_17725 {ECO:0000313|EMBL:POP51487.1};
OS Marortus luteolus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Spongiibacteraceae; Marortus.
OX NCBI_TaxID=2067667 {ECO:0000313|EMBL:POP51487.1, ECO:0000313|Proteomes:UP000237222};
RN [1] {ECO:0000313|EMBL:POP51487.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZX-21 {ECO:0000313|EMBL:POP51487.1};
RA Gaut B.S., Morton B.R., Clegg M.T., Duvall M.R.;
RL Submitted (JAN-2018) 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:POP51487.1}.
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DR EMBL; PQGG01000040; POP51487.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S4HC04; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000237222; 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}.
FT DOMAIN 17..438
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 459..732
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 778..899
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 958 AA; 104196 MW; 4EEC29864C9CC5C0 CRC64;
MTHTLTTLSQ SDDFLSRHIG PNEEQTAAML QAVGASSLDE LIQQTVPASI LRGDMPLPAP
QSESATLARL RTIAAKNQVA RSFIGTGYYG TITPPVILRN VLENPGWYTA YTPYQPEIAQ
GRLEALLNFQ QMVIDLTGLE LANASLLDEA TAAAEAMAMC KRSARKNKSD VFFVDRRCHP
QTIAVLKTRA LPLGLEIVVG DAETELVTTS CFGVLLQYPA TDGSISELSS IASQAKAQDA
MTVVAADIMS LILLTPPGEQ GADIVVGSAQ RFGVPMGFGG PHAAFFATRD SYKRSIPGRI
IGVSIDSRGN KALRMAMQTR EQHIRREKAT SNICTSQALL AIMAVFYAIY HGPDGLKTIA
QRINRMTGIF AAGLAQLGYS SNDAFFDTLT VNSGSASIAL ADKAEAELLN IRRGDNSVSI
SFDETTSTDD IEKLWQIFAG DKALPSIQAL DESLAELPGI PTNLRRQSSF LSHPVFHQHR
SETEMLRYMN RLERKDIALN HSMIALGSCT MKLNATTEMI PITWPEFGNM HPFAPRSQVA
GYLQLIDELE QQLIACTGYD KFSMQPNAGS QGEYAGLLAI KRYHESRGDF ARDICLIPSS
AHGTNPASAA MAGMRVVIVA CDELGNVDID DLRSKAERHA EQLSTLMVTY PSTHGVFEEG
IREICNITHQ HGGQVYVDGA NMNALVGLAA PGEFGADVSH LNLHKTFCIP HGGGGPGMGP
IGVKAHLAPF LPNHPVFPVE GLDAHNDTVS AASYGSAGIL PISWTYISLM GAAGLKKATQ
VAILNANYIA TRLKEHYPVL YTGRNDRVAH ECIIDLRPLK ESTGISEEDI AKRLMDYGFH
APTMSFPVPG TLMIEPTESE SKIELDRFCE AMIHIRREAG LVESGQLPAD NNPLVNAPHT
LADIVTDWDR PYSREEASFP VAQLRDGKYW PTVNRIDNVF GDRNLICSCP PIEMYLQD
//
