GCSPB_HALSA
ID GCSPB_HALSA Reviewed; 473 AA.
AC Q9HPK0;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=Probable glycine dehydrogenase (decarboxylating) subunit 2 {ECO:0000255|HAMAP-Rule:MF_00713};
DE EC=1.4.4.2 {ECO:0000255|HAMAP-Rule:MF_00713};
DE AltName: Full=Glycine cleavage system P-protein subunit 2 {ECO:0000255|HAMAP-Rule:MF_00713};
DE AltName: Full=Glycine decarboxylase subunit 2 {ECO:0000255|HAMAP-Rule:MF_00713};
DE AltName: Full=Glycine dehydrogenase (aminomethyl-transferring) subunit 2 {ECO:0000255|HAMAP-Rule:MF_00713};
GN Name=gcvPB {ECO:0000255|HAMAP-Rule:MF_00713}; Synonyms=gcvP2;
GN OrderedLocusNames=VNG_1601G;
OS Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS (Halobacterium halobium).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=64091;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX PubMed=11016950; DOI=10.1073/pnas.190337797;
RA Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA DasSarma S.;
RT "Genome sequence of Halobacterium species NRC-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
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:0000255|HAMAP-Rule:MF_00713}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-N(6)-lipoyl-L-lysyl-[glycine-cleavage complex H protein] +
CC glycine + H(+) = (R)-N(6)-(S(8)-aminomethyldihydrolipoyl)-L-lysyl-
CC [glycine-cleavage complex H protein] + CO2; 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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00713};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-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:0000255|HAMAP-Rule:MF_00713}.
CC -!- SIMILARITY: Belongs to the GcvP family. C-terminal subunit subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00713}.
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DR EMBL; AE004437; AAG19867.1; -; Genomic_DNA.
DR PIR; G84312; G84312.
DR RefSeq; WP_010903165.1; NC_002607.1.
DR AlphaFoldDB; Q9HPK0; -.
DR SMR; Q9HPK0; -.
DR STRING; 64091.VNG_1601G; -.
DR PaxDb; Q9HPK0; -.
DR EnsemblBacteria; AAG19867; AAG19867; VNG_1601G.
DR GeneID; 5954342; -.
DR KEGG; hal:VNG_1601G; -.
DR PATRIC; fig|64091.14.peg.1220; -.
DR HOGENOM; CLU_004620_5_0_2; -.
DR InParanoid; Q9HPK0; -.
DR OMA; MHINLHK; -.
DR OrthoDB; 8883at2157; -.
DR PhylomeDB; Q9HPK0; -.
DR Proteomes; UP000000554; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005960; C:glycine cleavage complex; IBA:GO_Central.
DR GO; GO:0016594; F:glycine binding; IBA:GO_Central.
DR GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IBA:GO_Central.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR HAMAP; MF_00713; GcvPB; 1.
DR InterPro; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR023012; GcvPB.
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; PTHR11773; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 3: Inferred from homology;
KW Oxidoreductase; Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..473
FT /note="Probable glycine dehydrogenase (decarboxylating)
FT subunit 2"
FT /id="PRO_0000167026"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 270
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00713"
SQ SEQUENCE 473 AA; 50487 MW; 665C7A7C655E22A7 CRC64;
MEHYEQARYA PAEGETNEPL LSENDQTTVS VDPSLPDDLT RDTVELPSLE EPELARHYVR
LSQQNYGVDS GPYPLGSCTM KYNPRFTEDA AALPAAAVHP DRSETALQGT LAVMHDLQDY
LGRIGGMDAV TLQPPAGAAG EFTGILIAEA YHEATDGGHR NEVIVPDAAH GTNFASAALG
GYDVIELPSG DDGRVDLDAL EAALGENTAA LMLTNPNTLG LFERDIEPIA EMVHDAGGLL
YYDGANLNAL LGRARPGDMG FDIMHFNVHK TFATPHGGGG PGAGPVGVTD ELAGFLPDPH
VRQSAGGDYE LYTPPRSIGK VHGFQGNWPV LVKAFAYIDR LGDSGLADAS AKAVLNANYL
ADQLDYEIPL GPFHHEFVAS AGDQDAADVA KRMLDYGVHP PTTKWPELVA EALMTEPTET
ESKRTLDDLA DAFNAVAGDD DAALADAPSR TTARRIDQTA AARNPRLSWH DLD
