ID A0A091D5Y3_FUKDA Unreviewed; 1164 AA.
AC A0A091D5Y3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Phosphoserine aminotransferase {ECO:0000256|RuleBase:RU004505};
DE EC=2.6.1.52 {ECO:0000256|RuleBase:RU004505};
GN ORFNames=H920_12707 {ECO:0000313|EMBL:KFO25903.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO25903.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO25903.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO25903.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + O-phospho-L-serine = 3-phosphooxypyruvate +
CC L-glutamate; Xref=Rhea:RHEA:14329, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:18110, ChEBI:CHEBI:29985, ChEBI:CHEBI:57524; EC=2.6.1.52;
CC Evidence={ECO:0000256|RuleBase:RU004505};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU004504};
CC -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from
CC 3-phospho-D-glycerate: step 2/3. {ECO:0000256|ARBA:ARBA00005099,
CC ECO:0000256|RuleBase:RU004505}.
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. SerC subfamily.
CC {ECO:0000256|ARBA:ARBA00006904}.
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DR EMBL; KN123317; KFO25903.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091D5Y3; -.
DR STRING; 885580.ENSFDAP00000013480; -.
DR eggNOG; KOG4308; Eukaryota.
DR UniPathway; UPA00135; UER00197.
DR UniPathway; UPA00244; UER00311.
DR Proteomes; UP000028990; Unassembled WGS sequence.
DR GO; GO:0004648; F:O-phospho-L-serine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006564; P:L-serine biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd00611; PSAT_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR HAMAP; MF_00160; SerC_aminotrans_5; 1.
DR InterPro; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
DR InterPro; IPR026212; Cep78.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR022278; Pser_aminoTfrase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR01364; serC_1; 1.
DR PANTHER; PTHR24110; CENTROSOMAL PROTEIN OF 78 KDA; 1.
DR PANTHER; PTHR24110:SF3; CENTROSOMAL PROTEIN OF 78 KDA; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR Pfam; PF13516; LRR_6; 2.
DR PRINTS; PR02062; CENTROSOME78.
DR SMART; SM00368; LRR_RI; 3.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR SUPFAM; SSF52047; RNI-like; 1.
DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW ECO:0000256|RuleBase:RU004505};
KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576,
KW ECO:0000256|RuleBase:RU004505}; Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000028990};
KW Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299,
KW ECO:0000256|RuleBase:RU004505};
KW Transferase {ECO:0000256|RuleBase:RU004505}.
FT DOMAIN 815..1151
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT REGION 429..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 563..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 655..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 453..497
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 571..588
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 682..701
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..717
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1164 AA; 128513 MW; 1D5302285C4C74C9 CRC64;
MIDSVKLRRD SAADFFSHYE YLCALQDSVP LPAVRACLRE GVLDFNADRL RVVDWAPLLS
TLKTNKDLPL ISIRSCFQPW LGETGSNINK VYRSRVPAIR SKDVTFQLCK ALKGCLNISS
VLRNLELNGL LLRERDLTIL TKGLNKSTSL VHLSLANCPI GDGGLEIICQ GIKNSITLKT
VNFTECNLTW QGADHMAKIL KYQVMRRHEE TWAESLRYRR PDLDCMAGLR RITLNCNTLV
GDLGARAFAD SLSEDLWLRA LDLQQCGLTN DGAQALLEAL ETNRTLVVLD IRRNPLIDHS
MMKAVIKKVL QNGRSAKSEY QWMTSPSVKE SPKTAKQKKR TIILGSSRKG KATIRIGLAT
KKPASSGRKY TLGKECYAPE PLPPGVSGFL PWRTAERAKR SRGFPLIKTR DIPTQLQPSD
FPVTVTVESP SSSEIEEIDD SSESVHEVPE KTSVKHEALQ EKLEECLKQL KEERVIRLKA
DKRVSELEHE NAQLRNINFS LSEALHAQSL THMILDDDGV LGSIENSFQK FHAFLDLLKD
AGLGQLATMA GIDQSDFHLL GRPQLNSTVS HPPEEEKKAP EEEKPDPKQS AAGQMQNIQF
QKITGDARIP LPLDSFHVPV STQETIVTSR DNLGNPAPEQ QQQQDSFEGF IARTCSPSAD
KIPGTGEEEW SRNSRSPSEK VTRAGEYTKK HSAKKQPGKD LHSYSDSSVS WKSKGTKENG
SLVKEPIKRG RSVSESPALL AFRVCGGRAG AGTAASCLEK PLHFLRDSRV LCGRGPVLAT
AEHLRPCNHV LLLPPRFISV ITATLLTSGS FEFLVLLELQ KELLDYRGVG ISVLEMSHRS
SDFGKIVGST ENLVRELLAV PDNYKVIFVQ GGGCGQFSAV PLNLIGLKAG RCADYVVTGA
WSAKAAEEAK KFGTVSIVHP KLGSYTKIPD PGTWTLNPDA SYVYFCANET VHGVEFDFIP
DVKGAVLVCD MSSNFLSRPV DVSKFGVIFA GAQKNVGCAG VTVVIVRDDL LGFALRECPS
VLEYKTQASS SSLYNTPPCF SIYVMGLVLE WIKNNGGAAN MEKLSSIKSK MIYDIIDRSQ
GFYVCPVEPQ NRSKMNVPFR IGSAKGDDAL EKRFLDKALE LNMISLKGHR SVGGIRVSLY
NAVTVEDVKK LAAFMENFLE MHQL
//
