ID A0A0K9NSL8_ZOSMR Unreviewed; 1042 AA.
AC A0A0K9NSL8;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Glycine cleavage system P protein {ECO:0000256|RuleBase:RU364056};
DE EC=1.4.4.2 {ECO:0000256|RuleBase:RU364056};
GN ORFNames=ZOSMA_70G00050 {ECO:0000313|EMBL:KMZ58990.1};
OS Zostera marina (Eelgrass).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Zosteraceae; Zostera.
OX NCBI_TaxID=29655 {ECO:0000313|EMBL:KMZ58990.1, ECO:0000313|Proteomes:UP000036987};
RN [1] {ECO:0000313|Proteomes:UP000036987}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Finnish {ECO:0000313|Proteomes:UP000036987};
RX PubMed=26814964; DOI=10.1038/nature16548;
RA Olsen J.L., Rouze P., Verhelst B., Lin Y.-C., Bayer T., Collen J.,
RA Dattolo E., De Paoli E., Dittami S., Maumus F., Michel G., Kersting A.,
RA Lauritano C., Lohaus R., Toepel M., Tonon T., Vanneste K., Amirebrahimi M.,
RA Brakel J., Bostroem C., Chovatia M., Grimwood J., Jenkins J.W.,
RA Jueterbock A., Mraz A., Stam W.T., Tice H., Bornberg-Bauer E., Green P.J.,
RA Pearson G.A., Procaccini G., Duarte C.M., Schmutz J., Reusch T.B.H.,
RA Van de Peer Y.;
RT "The genome of the seagrass Zostera marina reveals angiosperm adaptation to
RT the sea.";
RL Nature 530:331-335(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|ARBA:ARBA00004173,
CC ECO:0000256|RuleBase:RU364056}.
CC -!- SIMILARITY: Belongs to the GcvP family. {ECO:0000256|ARBA:ARBA00010756,
CC ECO:0000256|RuleBase:RU364056}.
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:KMZ58990.1}.
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DR EMBL; LFYR01001823; KMZ58990.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K9NSL8; -.
DR STRING; 29655.A0A0K9NSL8; -.
DR OMA; DEHCHPQ; -.
DR OrthoDB; 177349at2759; -.
DR Proteomes; UP000036987; Unassembled WGS sequence.
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|ARBA:ARBA00023128,
KW 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:UP000036987};
KW Transit peptide {ECO:0000256|RuleBase:RU364056}.
FT DOMAIN 83..510
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 522..803
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 854..975
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 776
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 1042 AA; 113464 MW; 716A33BAD9969FB7 CRC64;
MERARRLANR AILSRLVSQT KQSHHHHHSK IISSNRYISS LAPSIFFPAT RIPSERTTAH
HHNHQGRFIS IDALKPSDSF PRRHNSATPD EQSKMAELCG FSSLDALIDA TVPASIRIPE
MKFTGEFDAG FSESQMIAHM KYLADKNRVF KSFIGMGYYN THVPSVILRN IMENPAWYTQ
YTPYQAEIAQ GRLESLLNFQ TVVTDLTALP MSNASLLDEG TAAAEAMAMC NNIEKGKKKT
FFIASNCHPQ TIDICRTRAD GFDIKVVVTD LKDVDYSSKD VCGVLVQYPG TEGEVLDYGE
FVKTAHASGV KVVMASDLLA LTVLKPPGEF GVDIVIGSAQ RFGVPMGYGG PHAAFLATSQ
EYKRMMPGRI IGVSVDSAGK PALRMAMQTR EQHIRRGKAT SNICTAQALL ANMSAMFAVY
HGPGGLKDIA NRVHGLAGTF THGIKKLGTA TVQELPFFDT VKLTCSDADA VARLAAEHQI
NLRVVDSNTV TLAFDETTTL DDVDQLFKVF AGGKTVDFTA ASLAEEVQTC IPSGLTRETP
YLTNPIFNMY HTEHELLRYI HKLESKDLSL CHSMIPLGSC TMKLNATAEM LPVTWPSFAD
MHPFAPTDQT SGYQEMFEYL GELLCTITGF DSVSLQPNAG AAGEYTGLMA IRAYHLSKGD
DHRNVCIIPV SAHGTNPASA AMCGMKIVTI GTDSKGNINV DALRKAAEEN KDKLSAFMVT
YPSTHGVYEE GIDEICKIIH DNGGQVYMDG ANMNAQVGLT SPGYIGADVC HLNLHKTFCI
PHGGGGPGMG PIGVKKHLAP FLPSHPVVST GGIPASESVE PLGTISAAPW GSALILPISY
TYIAMMGSKG LTDASKIAIL NANYMAKRLE KEYPVLFRGE NGTCAHEFII DLRSFKNTVG
IEPEDVAKRL IDYGFHGPTM SWPVPGTLMI EPTESESKAE MDRFCDALIS IRGEIAEIEN
GKADIKDNVL KGAPHPPAML MSDTWTKPYS REYAAYPASW LRAAKFWPTT GRVDNVYGDR
NLVCTLPSSS HYVEESEAVA SA
//
