ID A3IKV0_9CHRO Unreviewed; 985 AA.
AC A3IKV0;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 100.
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=CY0110_22022 {ECO:0000313|EMBL:EAZ92819.1};
OS Crocosphaera chwakensis CCY0110.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Aphanothecaceae; Crocosphaera; Crocosphaera chwakensis.
OX NCBI_TaxID=391612 {ECO:0000313|EMBL:EAZ92819.1, ECO:0000313|Proteomes:UP000003781};
RN [1] {ECO:0000313|EMBL:EAZ92819.1, ECO:0000313|Proteomes:UP000003781}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCY0110 {ECO:0000313|EMBL:EAZ92819.1,
RC ECO:0000313|Proteomes:UP000003781};
RA Stal L., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (MAR-2007) 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:EAZ92819.1}.
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DR EMBL; AAXW01000004; EAZ92819.1; -; Genomic_DNA.
DR RefSeq; WP_008273963.1; NZ_AAXW01000004.1.
DR AlphaFoldDB; A3IKV0; -.
DR eggNOG; COG0403; Bacteria.
DR eggNOG; COG1003; Bacteria.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000003781; 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; 1.
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 33..459
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 804..925
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 725
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 985 AA; 108352 MW; EF9453B0604AF7DF CRC64;
MPNLDITANQ TQTNDNITSN LDNILSPTDR FSDRHIGPNS QEVDKMLKVL GFSTLDQLMD
AAVPKAIRLS KPLNLPEAQS EYAALAQLKS IASKNQIFRS YIGMGYYDCI TPPVIQRNIL
ENPGWYTAYT PYQAEIAQGR LEALLNYQTM IVELTGLEIA NASLLDEGTA AAEAMSMSYG
LCKNKKANAF FVDSHCHPQT IEVIKTRAYP LDIELIIADH RFFDFDTEIF GALLQYPATD
GSLYDYRTFI ETAHDQGAVV TVAADPLSLA LLTPPGEFGA DIAVGSTQRF GVPLGYGGPH
AAYFATKEAY KRQIPGRIVG VSKDAQGNPA LRLALQTREQ HIRREKATSN ICTAQVLLAV
IAGMYGVYHG AKGIKNIAQR IHKLTVILAK GLNKLSYTIN DEPFFDTVKV GVGDASAKAV
IKAAAERKIN LRLYKEGVLC ISLDETTTVH DVIELWQIFA AKDELPFTVK EIVQQVNFDF
PIFFKRTSNY LTDPVFNQHH SESELLRYLH QLENKDLALN TSMIPLGSCT MKLNAAAEMM
PVTWPEFGKL HPFAPLSQTE GYQILFQQLE EWLGEITGFD GISLQPNAGS QGEYAGLQVI
RQYHESRGET NRNICLIPES AHGTNPASAV MSGMKVVAVK CDKDGNIDIA DLEKKAEKHA
ENLGALMVTY PSTHGVFEEG IIDICNIIHR HGGQVYMDGA NMNAQVGLCR PADFGADVCH
LNLHKTFCIP HGGGGPGMGP IGVKEHLIPF LPTTNIEKYT NPDSNGNVET SIGAISAAPW
GSSSILAISW MYIAMMGEKG LTDATKVAIL NANYMASRLA DYYPILFKGA SGCVAHECII
DLRPLKKQAG VEVDDIAKRL MDFGFHAPTV SWPVIGTMMV EPTESEDLDE LDRFCDAMIT
IYHEVDAIAN GTIDPNNNPL KNAPHTAQAV ICGDWERPYS REKAAYPAPW TKEYKFWPVV
GRIDNAYGDR NLVCSCEGMD AYKED
//
