ID A9RLL8_PHYPA Unreviewed; 1038 AA.
AC A9RLL8;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE RecName: Full=Glycine cleavage system P protein {ECO:0000256|RuleBase:RU364056};
DE EC=1.4.4.2 {ECO:0000256|RuleBase:RU364056};
GN ORFNames=PHYPA_020459 {ECO:0000313|EMBL:PNR37351.1}, PHYPA_020461
GN {ECO:0000313|EMBL:PNR37353.1};
OS Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; Physcomitrium.
OX NCBI_TaxID=3218 {ECO:0000313|EMBL:PNR37351.1};
RN [1] {ECO:0000313|EMBL:PNR37351.1, ECO:0000313|Proteomes:UP000006727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c16_4520V3.1,
RC ECO:0000313|Proteomes:UP000006727};
RX PubMed=18079367; DOI=10.1126/science.1150646;
RA Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H.,
RA Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y., Tanahashi T.,
RA Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A.,
RA Suzuki Y., Hashimoto S.-I., Yamaguchi K., Sugano S., Kohara Y.,
RA Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B., Barker E.,
RA Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K., Estelle M.,
RA Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A., Hughes J.,
RA Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R., Pils B.,
RA Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J., Sanderfoot A.,
RA Schween G., Shiu S.-H., Stueber K., Theodoulou F.L., Tu H., Van de Peer Y.,
RA Verrier P.J., Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M.,
RA Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S.,
RA Boore J.L.;
RT "The Physcomitrella genome reveals evolutionary insights into the conquest
RT of land by plants.";
RL Science 319:64-69(2008).
RN [2] {ECO:0000313|EMBL:PNR37351.1, ECO:0000313|Proteomes:UP000006727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c16_4520V3.1,
RC ECO:0000313|Proteomes:UP000006727};
RX PubMed=29237241; DOI=10.1111/tpj.13801;
RA Lang D., Ullrich K.K., Murat F., Fuchs J., Jenkins J., Haas F.B.,
RA Piednoel M., Gundlach H., Van Bel M., Meyberg R., Vives C., Morata J.,
RA Symeonidi A., Hiss M., Muchero W., Kamisugi Y., Saleh O., Blanc G.,
RA Decker E.L., van Gessel N., Grimwood J., Hayes R.D., Graham S.W.,
RA Gunter L.E., McDaniel S.F., Hoernstein S.N.W., Larsson A., Li F.W.,
RA Perroud P.F., Phillips J., Ranjan P., Rokshar D.S., Rothfels C.J.,
RA Schneider L., Shu S., Stevenson D.W., Thummler F., Tillich M.,
RA Villarreal Aguilar J.C., Widiez T., Wong G.K., Wymore A., Zhang Y.,
RA Zimmer A.D., Quatrano R.S., Mayer K.F.X., Goodstein D., Casacuberta J.M.,
RA Vandepoele K., Reski R., Cuming A.C., Tuskan G.A., Maumus F., Salse J.,
RA Schmutz J., Rensing S.A.;
RT "The Physcomitrella patens chromosome-scale assembly reveals moss genome
RT structure and evolution.";
RL Plant J. 93:515-533(2018).
RN [3] {ECO:0000313|EnsemblPlants:Pp3c16_4520V3.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (DEC-2020) to UniProtKB.
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; ABEU02000016; PNR37351.1; -; Genomic_DNA.
DR EMBL; ABEU02000016; PNR37353.1; -; Genomic_DNA.
DR RefSeq; XP_001754864.1; XM_001754812.1.
DR AlphaFoldDB; A9RLL8; -.
DR STRING; 3218.A9RLL8; -.
DR PaxDb; 3218-PP1S15_499V6-1; -.
DR EnsemblPlants; Pp3c16_4520V3.1; Pp3c16_4520V3.1; Pp3c16_4520.
DR EnsemblPlants; Pp3c16_4520V3.2; Pp3c16_4520V3.2; Pp3c16_4520.
DR EnsemblPlants; Pp3c16_4550V3.1; Pp3c16_4550V3.1; Pp3c16_4550.
DR EnsemblPlants; Pp3c16_4550V3.2; Pp3c16_4550V3.2; Pp3c16_4550.
DR Gramene; Pp3c16_4520V3.1; Pp3c16_4520V3.1; Pp3c16_4520.
DR Gramene; Pp3c16_4520V3.2; Pp3c16_4520V3.2; Pp3c16_4520.
DR Gramene; Pp3c16_4550V3.1; Pp3c16_4550V3.1; Pp3c16_4550.
DR Gramene; Pp3c16_4550V3.2; Pp3c16_4550V3.2; Pp3c16_4550.
DR eggNOG; KOG2040; Eukaryota.
DR HOGENOM; CLU_004620_3_2_1; -.
DR InParanoid; A9RLL8; -.
DR OMA; DEHCHPQ; -.
DR OrthoDB; 177349at2759; -.
DR Proteomes; UP000006727; Chromosome 16.
DR GO; GO:0005960; C:glycine cleavage complex; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; 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 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 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 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:UP000006727};
KW Transit peptide {ECO:0000256|RuleBase:RU364056}.
FT DOMAIN 81..508
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 525..802
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 852..973
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 774
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 1038 AA; 112179 MW; 24DF2A38DDDDB93B CRC64;
MERAKQQVVK RLVQQAVRRA AAPSAPVRSG AALRAAAGNE TRRGFGASLL RGSGNGVVQL
PLGVRAISVE ALKPSDTFQR RHNSATLEEQ KAMAGMCGFE DMDAMIDATV PKSIRRPDLK
LSKYAEGLTE SELLAHFKSL ASKNKVMRSF IGMGYHDTHV PTVILRNILE NPGWYTQYTP
YQAEIAQGRL ESLLNFQTMI TDLTGMPMSN ASLLDEGTAA AEAMTMCSNI ARGRKKTFLV
ADNCHPQTIE VCKTRADGLG LNVVVADYKK FDYSSKDVSG VLVQYPATDG SVNDYSDFVK
NAHAHGVKVV MATDLLSLTV LTPPGELGAD MVVGSAQRFG VPMGYGGPHA AFLATSQEYK
RLMPGRIIGM SIDATGKPCL RMAMQTREQH IRRDKATSNI CTAQALLANM AAMYAVYHGP
EGLKTIANRV HGLAAVFSAG VSKLGFQTGS APFFDTVKVT VGEGQVEKVM KDAVAHGVNL
RQLDSSSVTL SFDETTTIGD VNTLFKIFGG GKNVGFTAEQ LAGEVESRLP SSLKRDTPFL
THPVFNQYHS EHELLRYLHR LQAKDLSLVH SMIPLGSCTM KLNATTEMIP ITWPEMANLH
PFAPEDQAQG YQEMFKELGD LLCEITGFDS MSLQPNAGAA GEYAGLMVIR AYHLARGDAH
RDVCIIPVSA HGTNPASAAM CGMRIVTVGT DKHGNVDIAE LRKAAEKHKD NLSALMVTYP
STHGVYEEGI DEICNIIHQY GGQVYMDGAN MNAQVGLTSP GHIGADVCHL NLHKTFCIPH
GGGGPGMGPI GVKKHLAPFL PSHPVVGTGG FPRPANTQPL GPISAAPYGS ALILPISYSY
IAMMGNKGLT DASKLAILNA NYMAKRLENH YPVLFRGVNG TCAHEFIIDL RKFKETAGIE
AEDVAKRLMD YGYHAPTMSW PVSGTLMIEP TESESKAELD RFCDALISIR EEIAAIENGE
ASREDNVLKG APHPASVVMA DDWTKSYSRE VAAFPASWVR ASKFWPTTSR VDNVYGDRNL
MCTNPSAEVI DEKIAAAA
//
