ID A0A317CJ35_9GAMM Unreviewed; 964 AA.
AC A0A317CJ35;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
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:PWQ98506.1};
GN ORFNames=DKT75_03375 {ECO:0000313|EMBL:PWQ98506.1};
OS Leucothrix arctica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Thiotrichaceae; Leucothrix.
OX NCBI_TaxID=1481894 {ECO:0000313|EMBL:PWQ98506.1, ECO:0000313|Proteomes:UP000245506};
RN [1] {ECO:0000313|EMBL:PWQ98506.1, ECO:0000313|Proteomes:UP000245506}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC9719 {ECO:0000313|EMBL:PWQ98506.1,
RC ECO:0000313|Proteomes:UP000245506};
RA Choi A., Baek K.;
RT "Leucothrix arctica sp. nov., isolated from Arctic seawater.";
RL Submitted (MAY-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:PWQ98506.1}.
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; QGKL01000011; PWQ98506.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A317CJ35; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000245506; 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:UP000245506}.
FT DOMAIN 20..443
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 486..750
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 786..907
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 713
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 964 AA; 105325 MW; 3737BA8F222E3E92 CRC64;
MKGSVPYSLQ TLEQHDDFVR RHNGPRVQDV EHMLSTIGAD SLDDLVNQTV PKKILSDQGL
ALGGACSEQE ALSALKAMAD QNIVATSYIG MGYYDTVVPP VILRNVLENP GWYTAYTPYQ
PEISQGRLEA LLNYQQVVTD LTGVDIANAS LLDEATAAAE AMSLCKRSNR LKTDKFFVDK
NIHPQTLDVL KTRAYHFGYE LIIGDAATEL VEHEVFGVLV QYPDTTGAIT DLQPLIDQAH
KQKALICVAA DLMSLLLLKS PGEMGADVVL GSAQRFGVPM GFGGPHAAFF AVRDKFKRTM
PGRLIGVSVD TKGNAALRMA LQTREQHIRR DKATSNICTA QALLANMASF YAVYHGPVRL
KQIAQRINRM ASIAALGLTQ KGIELANDTW FDTLTLNLGD KRDSVYAAAQ AKNINLRLMG
DDQVGISFDE RKTRQDLEML FDVILGEGHG LSVDTLDAAC TADNADCINA EYVRESEYLT
HAVFNTYHSE TEMLRYLKRL ENKDFSLTHG MIPLGSCTMK LNATSEMLPV TWPEFADIHP
FAPKEQTIGY RAMIADLETS LEEITGYDAI SMQPNSGAQG EYAGLVAISR YHESRGEGHR
NICLIPSSAH GTNPASAAML SQKVVIVECD ENGNVDIADF KAKAELHADN LASVMITYPS
THGVFEEAVV ELCEITHQFG GQVYMDGANL NAQVGLSKPG KFGSDVSHLN LHKTFCIPHG
GGGPGMGPIG VKSHLAPFLS SHVVSAVDDK VEGNSAVSAA PYGSAAILPI TWIYIKQMGA
EGLKRATELA ILNANYIMER LAPHYPVLFK GAQNRVAHEC IIDIRQIKVA SGITEEDIAK
RLMDYGFHAP TMSFPVAGTL MIEPTESESL GELDRFCDAM IAIKQEIDKV QAGGWPADNN
PLVNAPHTLR DLTEAWDHPY TQVDAVFPKG VLQTSKYWPT VSRVDNVYGD RNLVCDCPSI
DAYR
//
