ID A9RWB7_PHYPA Unreviewed; 482 AA.
AC A9RWB7;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE RecName: Full=Alanine-glyoxylate transaminase {ECO:0008006|Google:ProtNLM};
GN ORFNames=PHYPA_014274 {ECO:0000313|EMBL:PNR47154.1};
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:PNR47154.1};
RN [1] {ECO:0000313|EMBL:PNR47154.1, ECO:0000313|Proteomes:UP000006727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c10_22930V3.1,
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:PNR47154.1, ECO:0000313|Proteomes:UP000006727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c10_22930V3.1,
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:Pp3c10_22930V3.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (DEC-2020) to UniProtKB.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC ECO:0000256|RuleBase:RU003560}.
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DR EMBL; ABEU02000010; PNR47154.1; -; Genomic_DNA.
DR RefSeq; XP_001758348.1; XM_001758296.1.
DR AlphaFoldDB; A9RWB7; -.
DR STRING; 3218.A9RWB7; -.
DR PaxDb; 3218-PP1S32_198V6-1; -.
DR EnsemblPlants; Pp3c10_22930V3.1; Pp3c10_22930V3.1; Pp3c10_22930.
DR EnsemblPlants; Pp3c10_22930V3.2; Pp3c10_22930V3.2; Pp3c10_22930.
DR Gramene; Pp3c10_22930V3.1; Pp3c10_22930V3.1; Pp3c10_22930.
DR Gramene; Pp3c10_22930V3.2; Pp3c10_22930V3.2; Pp3c10_22930.
DR eggNOG; KOG1404; Eukaryota.
DR HOGENOM; CLU_016922_8_0_1; -.
DR InParanoid; A9RWB7; -.
DR OMA; REGLNQH; -.
DR OrthoDB; 345661at2759; -.
DR Proteomes; UP000006727; Chromosome 10.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0008453; F:alanine-glyoxylate transaminase activity; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009436; P:glyoxylate catabolic process; IBA:GO_Central.
DR GO; GO:0019481; P:L-alanine catabolic process, by transamination; IBA:GO_Central.
DR CDD; cd00610; OAT_like; 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 InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR45688; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1.
DR PANTHER; PTHR45688:SF3; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000006727}.
SQ SEQUENCE 482 AA; 52214 MW; 3AC5A018BCEA5C34 CRC64;
MAGGAIAGGR RLLLPRLQAL ASCRRGLSLA ADASKEVRPE AGVPQMPAFD YTPQPYDGPK
ADEILAKRKK FLNPALFLYY KKHLNIVEGK MQYLFDESGR RYLDAFAGIV TVSVGHGHPT
VVDAVVKQTK LLQHTTTIYL HHAIANYAEA LAQRMPGNLK VVYFVNSGSE ANDMAMMMAR
LYTGTFDIVS LRNAYHGMSP STMGLTAHST WKYNVAQGFG VHHVMNPDPY RGPFGADGKL
YANDLANLIE SATPGRIAGF FHETIQGVGG AVELAPGYLP AAYDIVRKAG GLCIADEVQT
GFGRTGSNFW GFQNQGVTPD IVTLAKGIGN GLPLAAVVTT PEIAQVLAQR LHFNTYGGNP
VCSAAGHAVL EVLEKEKRQA HCATVGDHLL HRLRALQDKH DIIGNVRGRG LMLGVELVKD
RTTKAPAKEE TLLLFEQLKD LGVLVGKGGL HGNVFRIKPP MCFSMEDADF LVDAMDHVMS
KL
//
