ID Q46HK2_PROMT Unreviewed; 382 AA.
AC Q46HK2;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE SubName: Full=NifS-like aminotransferase class-V {ECO:0000313|EMBL:AAZ59026.1};
GN OrderedLocusNames=PMN2A_1538 {ECO:0000313|EMBL:AAZ59026.1};
OS Prochlorococcus marinus (strain NATL2A).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC Prochlorococcaceae; Prochlorococcus.
OX NCBI_TaxID=59920 {ECO:0000313|EMBL:AAZ59026.1, ECO:0000313|Proteomes:UP000002535};
RN [1] {ECO:0000313|EMBL:AAZ59026.1, ECO:0000313|Proteomes:UP000002535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NATL2A {ECO:0000313|EMBL:AAZ59026.1,
RC ECO:0000313|Proteomes:UP000002535};
RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA Richardson P., Chisholm S.W.;
RT "Patterns and implications of gene gain and loss in the evolution of
RT Prochlorococcus.";
RL PLoS Genet. 3:2515-2528(2007).
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; CP000095; AAZ59026.1; -; Genomic_DNA.
DR RefSeq; WP_011294171.1; NC_007335.2.
DR AlphaFoldDB; Q46HK2; -.
DR STRING; 59920.PMN2A_1538; -.
DR KEGG; pmn:PMN2A_1538; -.
DR HOGENOM; CLU_003433_0_2_3; -.
DR OrthoDB; 9808002at2; -.
DR PhylomeDB; Q46HK2; -.
DR Proteomes; UP000002535; Chromosome.
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 GO; GO:0008483; F:transaminase activity; 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; 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.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:AAZ59026.1};
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:UP000002535};
KW Transferase {ECO:0000313|EMBL:AAZ59026.1}.
FT DOMAIN 8..367
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 382 AA; 41877 MW; 488D40CB9C52759C CRC64;
MDNNHLIFDF QSSTPCCTKV VEEMAPYWNE LWGNPSNTNN RSGVFASAAV EVSREKIASY
LNINPKRLIF TSGATEANNL GLVGHARAKA QLIGKPGHII TVSTEHHAVL DPLRQLQKEG
FRLTELHPNK EGLINIEQLS EAFEKDTFLV SVMAANNEIG VLQPIGDIGS FCKRKGIAFH
SDAAQAFGYL DLDPDKFRID LMSLSAHKIY GPKGIGALVI REGFPLEPSQ YGGGQELGLR
SGTLPVPLIV GFAKAVEITK NDQDERNKRL LFFRNLLLSG LKKNISGLIV NGSIDQRLPH
NLNITFPGVK GSQLHGQLRR FIFCTSGSAC SNGEASHVLQ EIGLSKKDAE ASIRMSIGRN
TTEKDINKAI NIITNIVINL RQ
//
