ID B3SFF8_TRIAD Unreviewed; 317 AA.
AC B3SFF8;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=Aminotransferase class V domain-containing protein {ECO:0000259|Pfam:PF00266};
GN ORFNames=TRIADDRAFT_35011 {ECO:0000313|EMBL:EDV18537.1};
OS Trichoplax adhaerens (Trichoplax reptans).
OC Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC Trichoplax.
OX NCBI_TaxID=10228 {ECO:0000313|EMBL:EDV18537.1, ECO:0000313|Proteomes:UP000009022};
RN [1] {ECO:0000313|EMBL:EDV18537.1, ECO:0000313|Proteomes:UP000009022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV18537.1,
RC ECO:0000313|Proteomes:UP000009022};
RX PubMed=18719581; DOI=10.1038/nature07191;
RA Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U.,
RA Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L.,
RA Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J.,
RA Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., Dellaporta S.L.,
RA Rokhsar D.S.;
RT "The Trichoplax genome and the nature of placozoans.";
RL Nature 454:955-960(2008).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU004504};
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. NifS/IscS subfamily.
CC {ECO:0000256|ARBA:ARBA00006490}.
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DR EMBL; DS986246; EDV18537.1; -; Genomic_DNA.
DR RefSeq; XP_002118977.1; XM_002118941.1.
DR AlphaFoldDB; B3SFF8; -.
DR STRING; 10228.B3SFF8; -.
DR EnsemblMetazoa; TriadT35011; TriadP35011; TriadG35011.
DR GeneID; 6760191; -.
DR KEGG; tad:TRIADDRAFT_35011; -.
DR CTD; 6760191; -.
DR eggNOG; KOG1549; Eukaryota.
DR HOGENOM; CLU_003433_0_1_1; -.
DR InParanoid; B3SFF8; -.
DR OMA; HINCAPP; -.
DR OrthoDB; 212394at2759; -.
DR PhylomeDB; B3SFF8; -.
DR Proteomes; UP000009022; Unassembled WGS sequence.
DR GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-EC.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
DR InterPro; IPR016454; Cysteine_dSase.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11601:SF34; CYSTEINE DESULFURASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11601; CYSTEINE DESULFURYLASE FAMILY MEMBER; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR PIRSF; PIRSF005572; NifS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000009022}.
FT DOMAIN 2..302
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EDV18537.1"
SQ SEQUENCE 317 AA; 35004 MW; 28A8836F551DF305 CRC64;
REIIFTSGAT ESDNLAIKGA VKHYANGKRR RVVTVKTEHK AVLDSVLALE REGFEVTFLD
VDQDGRLSVE EIEKNLGDDV VLLSVMHVNN ETGVVQDIKM IGNICRRYGV IFHVDAAQSA
GKLPINLKTL DVDLMSFSAH KLYGPKGVGA LYVSRNPRIN LQEQISGGGH ERGMRSGTIP
THQVVGMGMS FELAGERMSR DYEKFQVLAS LFWEEVRHLK GAVRNGGFTN TCPWIFNISV
PNVDAEAVMM SLKTLAISSG SACNSHKESS SHVLRAMNVS DALIESSFRF SFGRFTTESD
VAEAAERFVS VIKEWSY
//
