ID U2IZP4_9PORP Unreviewed; 961 AA.
AC U2IZP4;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=glycine dehydrogenase (aminomethyl-transferring) {ECO:0000256|ARBA:ARBA00012134};
DE EC=1.4.4.2 {ECO:0000256|ARBA:ARBA00012134};
GN ORFNames=HMPREF1556_00145 {ECO:0000313|EMBL:ERJ73272.1};
OS Porphyromonas sp. oral taxon 278 str. W7784.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=1227272 {ECO:0000313|EMBL:ERJ73272.1, ECO:0000313|Proteomes:UP000016628};
RN [1] {ECO:0000313|EMBL:ERJ73272.1, ECO:0000313|Proteomes:UP000016628}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W7784 {ECO:0000313|EMBL:ERJ73272.1,
RC ECO:0000313|Proteomes:UP000016628};
RA Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA Pepin K.H., Bhonagiri V., Zhang X., Warren W., Mitreva M., Mardis E.R.,
RA Wilson R.K.;
RL Submitted (JUN-2013) 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}.
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};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC 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}.
CC -!- SIMILARITY: Belongs to the GcvP family.
CC {ECO:0000256|ARBA:ARBA00010756}.
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:ERJ73272.1}.
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DR EMBL; AWUX01000016; ERJ73272.1; -; Genomic_DNA.
DR RefSeq; WP_021666489.1; NZ_KI259224.1.
DR AlphaFoldDB; U2IZP4; -.
DR STRING; 1227272.HMPREF1556_00145; -.
DR PATRIC; fig|1227272.3.peg.115; -.
DR eggNOG; COG0403; Bacteria.
DR eggNOG; COG1003; Bacteria.
DR HOGENOM; CLU_004620_3_2_10; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000016628; Unassembled WGS sequence.
DR GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0006546; P:glycine catabolic process; IEA:InterPro.
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 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};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR603437-50}.
FT DOMAIN 9..441
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 479..728
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 779..900
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 707
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 961 AA; 105995 MW; 7982867D3B496E77 CRC64;
MNTNDFSIRH IGVGQHEAQE MLQTIGVKSL DELIDQTLPS NIRLEKPLDL PEPMTEREFA
EHIADLASKN EVYTSYIGQG WYDTVLPPVI QRNVLESPVW YTSYTPYQAE ISQGRLEALF
NFQSVITDLT ALPLSNCSLL DEATAGAETA FLLFNERSKP KVKAEARKLF VDKDVFASTR
DVILTRCAPQ GIEVVLGKWQ EFDFGPEFFG AIVQYPGSLG GVNDYSEFVE KAHEADIKVG
VAADLLGLVL LTPPGEWGAD VVFGSAQRFG IPMYFGGPSA GYIACRTEYK RTLPGRIIGL
SKDRLGKPAY RLALQTREQH IKRERATSNI CTAQALLASM SGFYAIYHGP EGLKNIARRV
HSYAGFLAKK LTDLGYRLLH ENFFDTLCVI LPEEAGFADK LREIAEECRV NLFYAPCGTV
ALLSIDETTL PEDISVLCYI FASALGKESN FNDEVGEHTI HIDRKFVRTS PFLSYEVFNK
YHTETEMMRY IKRLERKDIS LTHSMISLGS CTMKLNAASE VIPLSNPAFC NVHPYAPAEQ
VQGSLELLEN LKSLLATITG LPVVSLQPNS GAAGEYAGLR TIRSYHEAHG GGHRNKVLLP
ASAHGTNPAS ASQCGYQCVI VACDEHGNVD WEDFMKKTEE HKDELAAMMI TYPSTHGIFE
TNIIDLCKRI HDCGALVYMD GANMNAQVGL TNPGFIGADV CHLNLHKTFA IPHGGGGPGS
GPICMTDALA PYQPTHGYGV DYEPIQGNVV AASPLGSAGI DVVSYAYIRL LGAKGLERAT
RTAILNANYL AVRLKDTYGI VYTGATGRVG HELILDCRKL KEVYGVDESD IAKRLMDFGY
HAPTLSFPVH GTLMIEPTES ESKDELDRFL AVMQCIWAEM QEIKDGKADA EDNVLKNAPH
PEYEVVSDSW SHSYPREKAA YPLEYLRENK FWINVARVDN GFGDRNLVPA FCACIAPSVE
G
//
