ID   D5U0N4_THEAM            Unreviewed;       519 AA.
AC   D5U0N4;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   RecName: Full=Probable glycine dehydrogenase (decarboxylating) subunit 2 {ECO:0000256|HAMAP-Rule:MF_00713};
DE            EC=1.4.4.2 {ECO:0000256|HAMAP-Rule:MF_00713};
DE   AltName: Full=Glycine cleavage system P-protein subunit 2 {ECO:0000256|HAMAP-Rule:MF_00713};
DE   AltName: Full=Glycine decarboxylase subunit 2 {ECO:0000256|HAMAP-Rule:MF_00713};
DE   AltName: Full=Glycine dehydrogenase (aminomethyl-transferring) subunit 2 {ECO:0000256|HAMAP-Rule:MF_00713};
GN   Name=gcvPB {ECO:0000256|HAMAP-Rule:MF_00713};
GN   OrderedLocusNames=Tagg_0409 {ECO:0000313|EMBL:ADG90684.1};
OS   Thermosphaera aggregans (strain DSM 11486 / M11TL).
OC   Archaea; Thermoproteota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Thermosphaera.
OX   NCBI_TaxID=633148 {ECO:0000313|EMBL:ADG90684.1, ECO:0000313|Proteomes:UP000002376};
RN   [1] {ECO:0000313|EMBL:ADG90684.1, ECO:0000313|Proteomes:UP000002376}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11486 / M11TL {ECO:0000313|Proteomes:UP000002376};
RX   PubMed=21304709;
RA   Spring S., Rachel R., Lapidus A., Davenport K., Tice H., Copeland A.,
RA   Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S.,
RA   Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.C., Brettin T.,
RA   Detter J.C., Tapia R., Han C., Heimerl T., Weikl F., Brambilla E.,
RA   Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Thermosphaera aggregans type strain (M11TL).";
RL   Stand. Genomic Sci. 2:245-259(2010).
RN   [2] {ECO:0000313|Proteomes:UP000002376}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11486 / M11TL {ECO:0000313|Proteomes:UP000002376};
RX   DOI=10.4056/sigs.821804;
RA   Spring S., Rachel R., Lapidus A., Davenport K., Tice H., Copeland A.,
RA   Cheng J.-F., Lucas S., Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S.,
RA   Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.-J., Jeffries C.C., Brettin T.,
RA   Detter J.C., Tapia R., Han C., Heimerl T., Weikl F., Brambilla E.,
RA   Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.-P.;
RT   "Complete genome sequence of Thermosphaera aggregans type strain
RT   (M11TLT).";
RL   Stand. Genomic Sci. 2:245-259(2010).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM 11486;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Spring S., Lapidus A., Munk C., Schroeder M., Glavina Del Rio T., Tice H.,
RA   Copeland A., Cheng J.-F., Lucas S., Chen F., Nolan M., Bruce D.,
RA   Goodwin L., Pitluck S., Ivanova N., Mavromatis K., Ovchinnikova G.,
RA   Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.-J.,
RA   Jeffries C.C., Brettin T., Detter J.C., Tapia R., Han C., Chain P.,
RA   Heimerl T., Weik F., Goker M., Rachel R., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.-P.;
RT   "Complete genome sequence of Thermosphaera aggregans type strain (M11TL).";
RL   Submitted (FEB-2010) 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|HAMAP-Rule:MF_00713}.
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_00713};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933, ECO:0000256|HAMAP-
CC         Rule:MF_00713};
CC   -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC       T, L and H. In this organism, the P 'protein' is a heterodimer of two
CC       subunits. {ECO:0000256|HAMAP-Rule:MF_00713}.
CC   -!- SIMILARITY: Belongs to the GcvP family. C-terminal subunit subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00713}.
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DR   EMBL; CP001939; ADG90684.1; -; Genomic_DNA.
DR   RefSeq; WP_013129277.1; NC_014160.1.
DR   AlphaFoldDB; D5U0N4; -.
DR   STRING; 633148.Tagg_0409; -.
DR   GeneID; 9165423; -.
DR   KEGG; tag:Tagg_0409; -.
DR   eggNOG; arCOG00076; Archaea.
DR   HOGENOM; CLU_004620_5_0_2; -.
DR   OrthoDB; 371967at2157; -.
DR   Proteomes; UP000002376; 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   Gene3D; 6.20.440.10; -; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   HAMAP; MF_00713; GcvPB; 1.
DR   InterPro; IPR023012; GcvPB.
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   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; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_00713}; Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_00713};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002376}.
FT   DOMAIN          108..300
FT                   /note="Glycine cleavage system P-protein N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02347"
FT   DOMAIN          370..471
FT                   /note="Glycine dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21478"
FT   MOD_RES         279
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00713"
SQ   SEQUENCE   519 AA;  57652 MW;  5C55EE753C527B5C CRC64;
     MFRQAKWSEP LIFELSVKGR RGFLVPEPEK EVKEKVGSIK LSEDMARTTD PDLPELSEVD
     VMRHFTRLTE MAYGVDNGPV PLGSCTMKYN PRIAWEVASD HRILGLHPLQ DEDTVQGLLE
     MIYEMQKWLA NITGMDYCSL HPAAGAHGEL AGILLIRKYH ELKGQIDKKT EIIVPDSAHG
     TNPASAAMGG FKVVEIPSNS DGNVDLEALK SVVGESTAGL MITNPSTLGL FEENILEIAR
     IIHSVDGLLY YDGANLNGIM GYARPGDMGF DIAHLNVHKT FGAPHGGGGP GAGPVCIKDR
     VVDAEKNIRL SDLLPGYYVI YDEKTGKYRL KGPGENSIGF LKAFFGNITP LIWGYTYILM
     MGNEGLRKVT ELAVLNTNYF IKLMENVKGY EIPYGKGRFR KHEVVLSAQP MTEELGVTAE
     DVAKGLLDAG FYAPTIYFPL IVKEALMTEF TETETIENIE KYAERLKEIS RIAYQDPKEP
     KKWPVNTSVG RIDLIKANHP STVTPTWRLH LKRVKGEIK
//