ID F0M1Q2_PSEPM Unreviewed; 961 AA.
AC F0M1Q2;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 76.
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 OrderedLocusNames=Asphe3_08000 {ECO:0000313|EMBL:ADX71998.1};
OS Pseudarthrobacter phenanthrenivorans (strain DSM 18606 / JCM 16027 / LMG
OS 23796 / Sphe3) (Arthrobacter phenanthrenivorans).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Pseudarthrobacter.
OX NCBI_TaxID=930171 {ECO:0000313|EMBL:ADX71998.1, ECO:0000313|Proteomes:UP000008639};
RN [1] {ECO:0000313|EMBL:ADX71998.1, ECO:0000313|Proteomes:UP000008639}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18606 / JCM 16027 / LMG 23796 / Sphe3
RC {ECO:0000313|Proteomes:UP000008639};
RX PubMed=21677849; DOI=10.4056/sigs.1393494;
RA Kallimanis A., Labutti K.M., Lapidus A., Clum A., Lykidis A.,
RA Mavromatis K., Pagani I., Liolios K., Ivanova N., Goodwin L., Pitluck S.,
RA Chen A., Palaniappan K., Markowitz V., Bristow J., Velentzas A.D.,
RA Perisynakis A., Ouzounis C.C., Kyrpides N.C., Koukkou A.I., Drainas C.;
RT "Complete genome sequence of Arthrobacter phenanthrenivorans type strain
RT (Sphe3).";
RL Stand. Genomic Sci. 4:123-130(2011).
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}.
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DR EMBL; CP002379; ADX71998.1; -; Genomic_DNA.
DR RefSeq; WP_013599938.1; NC_015145.1.
DR AlphaFoldDB; F0M1Q2; -.
DR STRING; 930171.Asphe3_08000; -.
DR KEGG; apn:Asphe3_08000; -.
DR eggNOG; COG0403; Bacteria.
DR eggNOG; COG1003; Bacteria.
DR HOGENOM; CLU_004620_2_1_11; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000008639; Chromosome.
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}.
FT DOMAIN 24..452
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 482..740
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 781..902
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 711
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 961 AA; 101357 MW; 96B86AE0A66C2511 CRC64;
MELLVTVTPA ASPATATAAA TFVDRHIGTR RQADVETMLK AVGYDTVDAL VDTAVPEDIR
QESVLELAGA LSEVEALAEL RRLAAKNKTA VQMIGQGYYD TVTPPVIRRN ILEGPAWYTA
YTPYQPEISQ GRLEALLNFQ TMVQDLVGLP IANASLLDEA TAVAEAVLMM RRANKNKDAR
DGKTVLDADC LPQTIAVVKG RAEALGFEVE VADLTAGLPD GAINGIVLQQ PGASGRVWDQ
SAVIAAAKER GALVTVAADL LALTLITPPG EQGADIAVGS AQRFGVPLFY GGPHAAYMAV
QKGLERSMPG RLVGVSKDSA GVPAYRLALQ TREQHIRREK ATSNICTAQA LLAIVASMYA
VYHGPEGLAA IARSAHVHAK TLAASLKAAG FEVRHTSFFD TVTVFVPGKA AGIIAAAEAQ
GINLRSIDAD TVGFSTDETT TAAIVDAVLA AFGVSSTADG DAALGLDAAV ERSSDFLQHP
VFNTHRSETQ LLRYIRKLSD RDLALDRTMI PLGSCTMKLN ATAEMEAISW PEFASIHPFA
PDSQTEGWRE LIADLEAQLT EITGYDQVSI QPNAGSQGEL AGLLAIRGYH HSRGEAQRNV
CLIPASAHGT NAASAVLAGM KVVVVATAAD GTIDHADLYA KIEANKDALS CIMITYPSTH
GVYDADVREV CDAVHAAGGQ VYIDGANLNA LVGLAQPGQF GGDVSHLNLH KTFCIPHGGG
GPGVGPVAAK AHLAPFMPGN AATWTEGNDV PISASKYGSA GVLPISWAYV KLMGGQGLTD
ATKSALLAAN YIAARLNDFF PVLYTGEGGL VAHECILDLR ELTARTGVTA EDVAKRLIDY
GFHAPTLAFP VAGTLMVEPT ESEDLGEMDR FIEAMISIRA EIDQVAAGDF TVTDSPLRNA
PHTAAAAISS DWDRAYPREQ AVFPVKSLKQ DKYFPPVGRI DGAAGDRNLI CSCPPLSEFE
N
//
