ID A0A0M2H1C1_9MICO Unreviewed; 961 AA.
AC A0A0M2H1C1;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
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:KJL40012.1};
GN ORFNames=RS81_01833 {ECO:0000313|EMBL:KJL40012.1};
OS Microbacterium ketosireducens.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=92835 {ECO:0000313|EMBL:KJL40012.1, ECO:0000313|Proteomes:UP000033956};
RN [1] {ECO:0000313|EMBL:KJL40012.1, ECO:0000313|Proteomes:UP000033956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12510 {ECO:0000313|EMBL:KJL40012.1,
RC ECO:0000313|Proteomes:UP000033956};
RA Corretto E.;
RT "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT metal contaminated environments.";
RL Submitted (FEB-2015) 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:KJL40012.1}.
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DR EMBL; JYIZ01000048; KJL40012.1; -; Genomic_DNA.
DR RefSeq; WP_045275762.1; NZ_JYIZ01000048.1.
DR AlphaFoldDB; A0A0M2H1C1; -.
DR STRING; 92835.RS81_01833; -.
DR PATRIC; fig|92835.4.peg.1855; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000033956; 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; 1.
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:UP000033956}.
FT DOMAIN 7..431
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 476..744
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 782..903
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 961 AA; 102034 MW; 5F1F94C945962E51 CRC64;
MTGAFAKRHI GVDDAARRTM LDALGYTDVD SLVKAAVPAS IHVVARSTSD IPPAATEAEA
LAELRALASQ NRAARPMIGL GYYDTFTPSV IARNVLENPS WYTAYTPYQP EISQGRLEAL
INFQTMVTDL TGLATANASM LDESTAVVEG MLVARRASKS TSNVFLVDPD ALPQTKALLE
HRAAAVGIEL VELADGHDAV EAFGAFVQYP GASGRIRDFS GVAAALHEQG GLVVAAADLL
ALTLLRSPGS LGADVAVGTT QRFGVPLGFG GPHAGYMAVR AGLERQLPGR LVGVSQDADG
HPAYRLSLQT REQHIRREKA TSNICTAQVL LAVMAAMYAV YHGPDGLRAI ATEVAQKAEA
LAGRLRSYGL TLQHDAFFDT IRVSVPGSAR RVVERARERG YQVLQVSDAV VGVSVDETTT
ADDLAAVAWA FGLPEVEFVG GGEQGERAVQ FAEASALAGV DASLHRVEEF LTHPVFNSHR
SETAMMRYLK QLADRDYALD RGMIPLGSCT MKLNAATEMA AVSWPEFSRV HPFAPEADVH
GYLAMIEQLE VWLAEVTGYD AVSLQPNAGS QGELAGLMAI RGYHRANGDL QRDVCLIPSS
AHGTNAASAV LAGMRVVVVA CDEAGNVDLD DLRAKIGVHA DALSALMITY PSTHGVYEHD
VLEITQAVHD AGGQVYVDGA NLNALLGYAR FGDLGGDVSH LNLHKTFAIP HGGGGPGVGP
VAAKAHLAPF LPGHPLAQRA DHAGGVFDAA GPISAAPYGS AGILPISWAY VRMMGLDGLR
EATAAAVLSA NYIAFRLKDH YPVLYAGEGG LVAHECILDL RPLREATGVT VDDVAKRLID
YGFHAPTMSF PVAGTLMVEP TESEDLGEIE RFIEAMIAIK VEADAVAAGE WAADDNPLVN
APHTAASVIE GEWEHPYPRS TAVYPVHSLV RTKYWPPVRR IDQAYGDRNL VCSCPPPEAF
A
//