ID   PIGE_SERS3              Reviewed;         853 AA.
AC   Q5W267;
DT   11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Aminotransferase PigE {ECO:0000303|PubMed:15853884};
DE            EC=2.6.1.- {ECO:0000305|PubMed:15853884};
GN   Name=pigE {ECO:0000303|PubMed:15528645};
OS   Serratia sp. (strain ATCC 39006).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia; unclassified Serratia.
OX   NCBI_TaxID=104623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 39006 / SC 11482;
RX   PubMed=15528645; DOI=10.1099/mic.0.27222-0;
RA   Harris A.K., Williamson N.R., Slater H., Cox A., Abbasi S., Foulds I.,
RA   Simonsen H.T., Leeper F.J., Salmond G.P.;
RT   "The Serratia gene cluster encoding biosynthesis of the red antibiotic,
RT   prodigiosin, shows species- and strain-dependent genome context
RT   variation.";
RL   Microbiology 150:3547-3560(2004).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, AND PATHWAY.
RC   STRAIN=ATCC 39006 / SC 11482;
RX   PubMed=15853884; DOI=10.1111/j.1365-2958.2005.04602.x;
RA   Williamson N.R., Simonsen H.T., Ahmed R.A., Goldet G., Slater H.,
RA   Woodley L., Leeper F.J., Salmond G.P.;
RT   "Biosynthesis of the red antibiotic, prodigiosin, in Serratia:
RT   identification of a novel 2-methyl-3-n-amyl-pyrrole (MAP) assembly pathway,
RT   definition of the terminal condensing enzyme, and implications for
RT   undecylprodigiosin biosynthesis in Streptomyces.";
RL   Mol. Microbiol. 56:971-989(2005).
CC   -!- FUNCTION: Involved in the biosynthesis of 2-methyl-3-n-amyl-pyrrole
CC       (MAP), one of the terminal products involved in the biosynthesis of the
CC       red antibiotic prodigiosin (Pig). Catalyzes the transamination to the
CC       aldehyde group of 3-acetyloctanal, resulting in an aminoketone, which
CC       spontaneously cyclizes to yield the dihydro form of MAP (H2MAP).
CC       {ECO:0000269|PubMed:15853884}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250|UniProtKB:A0A0J9X1Q5};
CC   -!- PATHWAY: Antibiotic biosynthesis; prodigiosin biosynthesis.
CC       {ECO:0000305|PubMed:15853884}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:A0A0J9X1Q5}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene show a white phenotype
CC       and produce 4-hydroxy-2,2'-bipyrrole-5-carbaldehyde (HBC), 4- methoxy-
CC       2,2'-bipyrrole-5-carbaldehyde (MBC) and 4-hydroxy-2,2'-bipyrrole-5-
CC       methanol (HBM). {ECO:0000269|PubMed:15853884}.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; AJ833001; CAH55633.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5W267; -.
DR   SMR; Q5W267; -.
DR   STRING; 104623.Ser39006_01373; -.
DR   KEGG; ag:CAH55633; -.
DR   eggNOG; COG4992; Bacteria.
DR   eggNOG; COG5322; Bacteria.
DR   UniPathway; UPA01072; -.
DR   GO; GO:0070280; F:pyridoxal binding; ISS:UniProtKB.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IMP:UniProtKB.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IMP:UniProtKB.
DR   CDD; cd00610; OAT_like; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 2.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   1: Evidence at protein level;
KW   Aminotransferase; Antibiotic biosynthesis; Pyridoxal phosphate;
KW   Transferase.
FT   CHAIN           1..853
FT                   /note="Aminotransferase PigE"
FT                   /id="PRO_0000436241"
FT   BINDING         503..504
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0J9X1Q5"
FT   BINDING         680
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0J9X1Q5"
FT   MOD_RES         645
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0J9X1Q5"
SQ   SEQUENCE   853 AA;  93577 MW;  9C26F2E250F057D7 CRC64;
     MKFGFIAHPT SVGLKRYVKM IDLLQRNSTE LHSGYKRDLW RRENLVPFMN FAKITSATGA
     TCEGVIKYMP LVADEMLADA RGIANRVVSG IEELVEDGAE LVGLGGFTSI VGRRGEATAE
     KSPVPVTSGN SLTTYAGYKA LMQIQSWLDI QPEQEPVAIV GYPGSICLAL SRLLLAQGFS
     LHLLHRAGHK DEDELLSHLP EQYRSRVTLT SDPEDLYPRC KLFVAATSAG GVIDPYKLQP
     GSVFIDVALP RDINSDTRPD RDDILIIDGG CVTATDAVKL GGESLNVTIK QQLNGCMAET
     IVLALENRRE NFSLGRYLAL DNVLEIGELA EKHGFLVYPL ASYGERIDRQ RVINLKRYYH
     HDIYSDEPDT EQPPASQLAF IDAIIAQDPA REDTLDRYHQ FINPMMVEFL KLQHCDNVFR
     RASGTQLFTA DGEAFLDMVA GYGCINLGHN PQPIIDALKA YLDAQGPNFI QYISIPEQAA
     KLAEVLCHFA PGNMGRVFFS NSGTEAVEAA MKLAKASTGK AGIAYLKNSY HGKTLGALSI
     TGREKHRRHF KPLLASMIEV PFADIEALRQ TLSRDDIGAL MIEPIQGEGG VHVPPPGYLR
     TVQEICRQTD TLLMVDEVQT GLGRTGKLFA CEWEGIEPDV LMLSKSLSGG VMPIGATLCR
     AIFGNGPYGT ADRFLMHSST FGGGNIAAVV ALSALREILA QDLVGNAERL GTYFKQALTD
     VAARYPFVAE IAGRGLMLGI QFDQTFAGAV GASAREFATR LPGDWHTTWK FLPDPVQAHL
     KAAMERMEQS LGEMFCMKFV TKLCQDHNIL TFITANSSTV IRIQPPLTIS KAEIDRFVSA
     FATVCDELST FLE