ID A0A2T1C3X1_9CYAN Unreviewed; 991 AA.
AC A0A2T1C3X1;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
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:PSB02868.1};
GN ORFNames=C7B64_11225 {ECO:0000313|EMBL:PSB02868.1};
OS Merismopedia glauca CCAP 1448/3.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Merismopediaceae;
OC Merismopedia.
OX NCBI_TaxID=1296344 {ECO:0000313|EMBL:PSB02868.1, ECO:0000313|Proteomes:UP000238762};
RN [1] {ECO:0000313|EMBL:PSB02868.1, ECO:0000313|Proteomes:UP000238762}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCAP 1448/3 {ECO:0000313|EMBL:PSB02868.1,
RC ECO:0000313|Proteomes:UP000238762};
RA Cohen D.B., Kent A.D.;
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PSB02868.1, ECO:0000313|Proteomes:UP000238762}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCAP 1448/3 {ECO:0000313|EMBL:PSB02868.1,
RC ECO:0000313|Proteomes:UP000238762};
RA Moore K.R., Magnabosco C., Momper L., Gold D.A., Bosak T., Fournier G.P.;
RT "The ancient ancestry and fast evolution of plastids.";
RL Submitted (MAR-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:PSB02868.1}.
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DR EMBL; PVWJ01000047; PSB02868.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T1C3X1; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000238762; 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:SF1; GLYCINE DEHYDROGENASE (DECARBOXYLATING), MITOCHONDRIAL; 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:UP000238762}.
FT DOMAIN 48..472
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 511..766
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 812..933
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 740
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 991 AA; 108776 MW; 65913F842718318C CRC64;
MSDSSNYEQL IPSIDRNRPV KPSVDRVESN SWVTPSADWQ LGDEFLWRHI GPQPEDIAQM
LSFLGFSSLD ELIDRTVPSQ IRQQEGLSLI KSGTESQVLT SLRAIASQNQ VFRSFIGMGY
YNCITPGVIQ RNILENPGWY TQYTPYQPEI SQGRLEALLN FQTMVIDLTG MEIANSSLLD
EGTAAAEAMT MAYNAQGKNP VKTFWVSQDC HPQTIAVVET RAKYLGVEVI IGDYKTWDFT
QKIFGILLQY PATDGAIYDY QEFVAKGHEK GALAIVAADL LSLTLLKPPG EWGADVVVGN
TQRFGVPLGY GGPHAAYFAT KEAYKRQIPG RLVGVSKDNR GEVALRLALQ TREQHIRRDK
ATSNICTAQV LLAVMASMYA VYHGSEGLKR IALRIHGWTS VLATGLEKLG YEVGKAPFFD
TIKVKVPGTA SQILAKATAN SLNLREIDSQ TIGISLDETT TKIDIIDLLE IFAVDGNLTF
SVEEISQHHL AELSIIKGFE RTSKYLTHPV FNTHHSETEL LRYMQRLQNK DLSLTHSMIP
LGSCTMKLNA TAEMIPVTWA EFGQIHPFVP IEQTKGYQIL FQQLEKWLAE ITGFAAISLQ
PNAGSQGEYA GLLVISQYHA QKGDISRNIC LIPQSAHGTN PASAVMAGMQ VVAVACDDEG
NIDVADLQAK AEKHKDNLAA LMVTYPSTHG VFEESIQEIC QIVHDCGGQV YMDGANLNAQ
VGLCRPGDIG ADVCHLNLHK TFCIPHGGGG PGMGPIGVAA HLAPFLPKHP VIKVGGEQGI
GAIASSPWSS ASILPISWVY IALMGASGLQ KATQVAILNA NYIAKRLEAY YPILYKGKNG
LVAHECILDL RQFKKTADID VDDIAKRLID YGFHPPTVSW PVAGTIMVEP TESESKEELD
RFCEAMIAIR AEIRGIELGE VDKANNVLKN APHTIADLTA IEWNRPYSRE KAVYPTDAVK
KHKFWATVNR IDQAYGDRNL VCSCPSMAAY S
//
