PIGE_SERSF
ID PIGE_SERSF Reviewed; 853 AA.
AC A0A0J9X1Q5; A0A0H2UKZ2;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2015, sequence version 1.
DT 03-AUG-2022, entry version 29.
DE RecName: Full=Aminotransferase PigE {ECO:0000303|PubMed:24704447};
DE EC=2.6.1.- {ECO:0000250|UniProtKB:Q5W267};
GN Name=pigE {ECO:0000303|PubMed:24704447};
GN ORFNames=L085_23050 {ECO:0000312|EMBL:AIA50007.1};
OS Serratia sp. (strain FS14).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia; unclassified Serratia.
OX NCBI_TaxID=1327989;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FS14;
RX PubMed=25856195; DOI=10.1371/journal.pone.0123061;
RA Li P., Kwok A.H., Jiang J., Ran T., Xu D., Wang W., Leung F.C.;
RT "Comparative genome analyses of Serratia marcescens FS14 reveals its high
RT antagonistic potential.";
RL PLoS ONE 10:E0123061-E0123061(2015).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE,
RP FUNCTION, COFACTOR, AND SUBUNIT.
RC STRAIN=FS14;
RX PubMed=24704447; DOI=10.1016/j.bbrc.2014.03.125;
RA Lou X., Ran T., Han N., Gao Y., He J., Tang L., Xu D., Wang W.;
RT "Crystal structure of the catalytic domain of PigE: a transaminase involved
RT in the biosynthesis of 2-methyl-3-n-amyl-pyrrole (MAP) from Serratia sp.
RT FS14.";
RL Biochem. Biophys. Res. Commun. 447:178-183(2014).
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:24704447}.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:24704447};
CC -!- PATHWAY: Antibiotic biosynthesis; prodigiosin biosynthesis.
CC {ECO:0000250|UniProtKB:Q5W267, ECO:0000305}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:24704447}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; CP005927; AIA50007.1; -; Genomic_DNA.
DR RefSeq; WP_015376883.1; NZ_CP005927.1.
DR PDB; 4PPM; X-ray; 2.30 A; A/B=1-853.
DR PDBsum; 4PPM; -.
DR AlphaFoldDB; A0A0J9X1Q5; -.
DR SMR; A0A0J9X1Q5; -.
DR KEGG; serf:L085_23050; -.
DR PATRIC; fig|1327989.4.peg.3250; -.
DR HOGENOM; CLU_016845_0_0_6; -.
DR BioCyc; MetaCyc:MON-18837; -.
DR UniPathway; UPA01072; -.
DR GO; GO:0070280; F:pyridoxal binding; IDA:UniProtKB.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IDA:UniProtKB.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IDA:UniProtKB.
DR CDD; cd00610; OAT_like; 1.
DR DisProt; DP00913; -.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
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 3D-structure; Aminotransferase; Antibiotic biosynthesis;
KW Pyridoxal phosphate; Transferase.
FT CHAIN 1..853
FT /note="Aminotransferase PigE"
FT /id="PRO_0000436242"
FT BINDING 503..504
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:24704447"
FT BINDING 680
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:24704447"
FT MOD_RES 645
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000269|PubMed:24704447"
FT HELIX 377..386
FT /evidence="ECO:0007829|PDB:4PPM"
FT HELIX 391..401
FT /evidence="ECO:0007829|PDB:4PPM"
FT HELIX 404..412
FT /evidence="ECO:0007829|PDB:4PPM"
FT STRAND 419..424
FT /evidence="ECO:0007829|PDB:4PPM"
FT STRAND 426..429
FT /evidence="ECO:0007829|PDB:4PPM"
FT STRAND 434..440
FT /evidence="ECO:0007829|PDB:4PPM"
FT HELIX 441..443
FT /evidence="ECO:0007829|PDB:4PPM"
FT HELIX 452..463
FT /evidence="ECO:0007829|PDB:4PPM"
FT TURN 471..473
FT /evidence="ECO:0007829|PDB:4PPM"
FT HELIX 477..489
FT /evidence="ECO:0007829|PDB:4PPM"
FT STRAND 490..492
FT /evidence="ECO:0007829|PDB:4PPM"
FT STRAND 496..502
FT /evidence="ECO:0007829|PDB:4PPM"
FT HELIX 503..518
FT /evidence="ECO:0007829|PDB:4PPM"
FT STRAND 522..526
FT /evidence="ECO:0007829|PDB:4PPM"
FT HELIX 535..538
FT /evidence="ECO:0007829|PDB:4PPM"
FT HELIX 544..547
FT /evidence="ECO:0007829|PDB:4PPM"
FT STRAND 557..560
FT /evidence="ECO:0007829|PDB:4PPM"
FT HELIX 565..573
FT /evidence="ECO:0007829|PDB:4PPM"
FT STRAND 577..582
FT /evidence="ECO:0007829|PDB:4PPM"
FT STRAND 584..586
FT /evidence="ECO:0007829|PDB:4PPM"
FT TURN 587..590
FT /evidence="ECO:0007829|PDB:4PPM"
FT HELIX 598..608
FT /evidence="ECO:0007829|PDB:4PPM"
FT STRAND 612..616
FT /evidence="ECO:0007829|PDB:4PPM"
FT TURN 618..625
FT /evidence="ECO:0007829|PDB:4PPM"
FT STRAND 626..629
FT /evidence="ECO:0007829|PDB:4PPM"
FT HELIX 630..633
FT /evidence="ECO:0007829|PDB:4PPM"
FT STRAND 639..643
FT /evidence="ECO:0007829|PDB:4PPM"
FT HELIX 645..648
FT /evidence="ECO:0007829|PDB:4PPM"
FT TURN 649..651
FT /evidence="ECO:0007829|PDB:4PPM"
FT STRAND 655..659
FT /evidence="ECO:0007829|PDB:4PPM"
FT HELIX 661..668
FT /evidence="ECO:0007829|PDB:4PPM"
FT TURN 671..675
FT /evidence="ECO:0007829|PDB:4PPM"
FT HELIX 685..700
FT /evidence="ECO:0007829|PDB:4PPM"
FT HELIX 703..722
FT /evidence="ECO:0007829|PDB:4PPM"
FT STRAND 726..734
FT /evidence="ECO:0007829|PDB:4PPM"
FT STRAND 737..742
FT /evidence="ECO:0007829|PDB:4PPM"
FT HELIX 767..770
FT /evidence="ECO:0007829|PDB:4PPM"
FT HELIX 774..807
FT /evidence="ECO:0007829|PDB:4PPM"
FT STRAND 818..823
FT /evidence="ECO:0007829|PDB:4PPM"
FT HELIX 831..851
FT /evidence="ECO:0007829|PDB:4PPM"
SQ SEQUENCE 853 AA; 93256 MW; 57A8F0F3D2BC96F2 CRC64;
MKFGFIAHPT SLGLKRYVKM LDLLQRNSTE QHSGYTRELW ERQNLVPFMN FARITSATGA
TCEGVIKYMP LVADEMLADA RGIAARVVQG IEELAGDGAE LVGLGGFTSI VGRRGEATAE
KSPVPVTSGN SLTTYAGYKA LMQIQSWLEI RPEEEPVAIV GYPGSICLAL SRLLLAHGFS
LHLLHRAGNH DRSELLSHLP EEYHSRVTLT SDPEDLYPRC KLFAAATSAG GVIDPARLQP
GSIFIDVALP RDIASETRPA RDDILIIDGG CVTATDAVKL GGESLNVTIK QQLNGCMAET
IVLALENRRE NFSLGRYLAP EKVLEIGEIA ERHGFFAYPL ASYGERIDRQ SVTNLKRYYH
HDIYAGESAD AALPASRLAF IDAVIAQTPA REDTLDRYHQ YINPMMVDFL KLQRCDNVFR
SAAGTQLYDD AGEAFLDMVA GYGCLNLGHN PQPVVNALKN YLDAQGPNFI QYISIPEQTA
KLAEVLCRLA PGNMGRVFFS NSGTEAVEAA MKIAKASTGK PGIAYLRNSY HGKTLGALSI
TGRDKHRRYF TPLLDAMVEV PFGDLAALRE ALNREDVGAL MIEPIQGEGG VHIPPAGYLQ
AVQQLCRETG VLLMVDEVQT GLGRTGKLFA CEWDGIEPDV LMLSKSLSGG LIPIGATLCR
ADLWQKAYGT ADRFLVHSST YGGGNLASVV ALSALREILA QDLVGHAERM GAYFKQALSE
IAARYPFVSE VRGRGLMLGI QFDQAFTGAV NASAREFATR LPGDWHTTWK FLPDPVQAHL
RAAMDRMEQA LGEMFCMKFV TKLCQDHKIL TFITANSSTV IRIQPPLIIS KAEIDRFVGA
FATVCEELST FLD
