ID A0A1E3PGI4_9ASCO Unreviewed; 944 AA.
AC A0A1E3PGI4;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Glycine cleavage system P protein {ECO:0000256|RuleBase:RU364056};
DE EC=1.4.4.2 {ECO:0000256|RuleBase:RU364056};
GN ORFNames=NADFUDRAFT_26772 {ECO:0000313|EMBL:ODQ64519.1};
OS Nadsonia fulvescens var. elongata DSM 6958.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetales incertae sedis; Nadsonia.
OX NCBI_TaxID=857566 {ECO:0000313|EMBL:ODQ64519.1, ECO:0000313|Proteomes:UP000095009};
RN [1] {ECO:0000313|EMBL:ODQ64519.1, ECO:0000313|Proteomes:UP000095009}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6958 {ECO:0000313|EMBL:ODQ64519.1,
RC ECO:0000313|Proteomes:UP000095009};
RX PubMed=27535936; DOI=10.1073/pnas.1603941113;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goeker M.,
RA Salamov A.A., Wisecaver J.H., Long T.M., Calvey C.H., Aerts A.L.,
RA Barry K.W., Choi C., Clum A., Coughlan A.Y., Deshpande S., Douglass A.P.,
RA Hanson S.J., Klenk H.-P., LaButti K.M., Lapidus A., Lindquist E.A.,
RA Lipzen A.M., Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J.L.,
RA Peng Y., Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C.,
RA Stielow J.B., Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V.,
RA Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:9882-9887(2016).
CC -!- FUNCTION: The glycine cleavage system catalyzes the degradation of
CC glycine. {ECO:0000256|RuleBase:RU364056}.
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 ECO:0000256|RuleBase:RU364056};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR603437-50, ECO:0000256|RuleBase:RU364056};
CC -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC T, L and H. {ECO:0000256|RuleBase:RU364056}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|RuleBase:RU364056}.
CC -!- SIMILARITY: Belongs to the GcvP family. {ECO:0000256|ARBA:ARBA00010756,
CC ECO:0000256|RuleBase:RU364056}.
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DR EMBL; KV454411; ODQ64519.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E3PGI4; -.
DR STRING; 857566.A0A1E3PGI4; -.
DR OrthoDB; 177349at2759; -.
DR Proteomes; UP000095009; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IEA:UniProtKB-UniRule.
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 Mitochondrion {ECO:0000256|RuleBase:RU364056};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU364056};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR603437-50,
KW ECO:0000256|RuleBase:RU364056};
KW Reference proteome {ECO:0000313|Proteomes:UP000095009};
KW Transit peptide {ECO:0000256|RuleBase:RU364056}.
FT DOMAIN 1..420
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 427..710
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 766..887
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 686
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 944 AA; 102796 MW; F2C8018314E65176 CRC64;
MLKTVGYPSL DKFVEAVVPR DILTNRPLQV EPVNGYTENE LTTRLKEIAS QNKIFKTYIG
QGYSGTIVPP VIQRNILECP EWYTSYTPYQ PEISQGRLES LLNFQTMVAD LTGMSVSNAS
LLDEGTAAAE AVIMSFHAAK GKKKTYYVDP SVNSQTINVV QSRATPLGIN VVIGKPPATD
ATNAKKDYKD VIGCLVQYPA TDGSLTNWSE LSANIHASGG LLSVASDLLA LTLIEPPSKF
GADIVLGSSQ RFGVPMGYGG PHAAFFAVAD GQKRKMPGRL IGKSKDRLGN DAYRLALQTR
EQHIKREKAT SNICTAQALL ANMAAMYAVY HGPQGLKDIA SRVFTLTSIL AASIKNTPGL
ELVNQNWFDT LTIKVASSQA IIDKALAKQV NLYQIDPTTI SISLDETVSE ADLVQLIEIL
GSQELSASLN SLGLTQQFAH VDTAFQRSSE FLRHDVFNKY HTETELLRYV HHLQSKDLSL
ANSMIPLGSC TMKLNATTQM APISWPEFSN LHPFVPLEQA QGYKVLLQEL EADLAEITGF
DNVSLQPNSG AQGEYAGLRV IKAYLESTGQ GHRDICLIPV SAHGTNPASA VMAGMKVISI
KCTANGELDL PDMIVKAEQY KDRLAAVMIT YPSTFGVFEP GVKKAIDIVH SHGGQVYMDG
ANMNAQIGLT SPGEIGADVC HLNLHKTFCI PHGGGGPGMG PICVKSHLGP FLPSHPTVDM
SEVKGELIDP AKAIQSISAA PWGSASILPI SWAYIKLMGG AGLAKATKVA LLNANYMMDK
LRPHYPILYT NDENRCAHEF ILDVRGFKET SGVEAIDIAK RLQDYGFHGP TMSWPVANTL
MIEPTESESL AELDRFCDAL IAIRAEISEI EAGSMPRQNN ALKNSPHSTK DLLSAEWDRP
YSREKAAFPL PYLLERKFWP SVTRLDDTYG DMNLFCTCEP PALD
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