PIGH_SERS3
ID PIGH_SERS3 Reviewed; 653 AA.
AC Q5W264;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=4-hydroxy-2,2'-bipyrrole-5-methanol synthase PigH {ECO:0000305};
DE Short=HBM synthase {ECO:0000305};
DE EC=2.3.2.- {ECO:0000305|PubMed:15853884, ECO:0000305|PubMed:17002325};
DE AltName: Full=Aminotransferase PigH {ECO:0000303|PubMed:17002325};
GN Name=pigH {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).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF SER-45 AND SER-139, COFACTOR,
RP PATHWAY, AND PHOSPHOPANTETHEINYLATION AT SER-45.
RC STRAIN=ATCC 39006 / SC 11482;
RX PubMed=17002325; DOI=10.1021/ja063611l;
RA Garneau-Tsodikova S., Dorrestein P.C., Kelleher N.L., Walsh C.T.;
RT "Protein assembly line components in prodigiosin biosynthesis:
RT characterization of PigA,G,H,I,J.";
RL J. Am. Chem. Soc. 128:12600-12601(2006).
CC -!- FUNCTION: Involved in the biosynthesis of 4-methoxy-2,2'-bipyrrole-5-
CC carbaldehyde (MBC), one of the terminal products involved in the
CC biosynthesis of the red antibiotic prodigiosin (Pig). Carrier of the L-
CC malonyl group (malonyl-S-PigH), which is decarboxylated by PigJ to
CC yield a C2 carbanion acetyl-S-PigH. Then the pyrrolyl group of
CC pyrrolyl-S-cysteinyl PigJ intermediate is captured by the C2 carbanion
CC acetyl-S-PigH to yield the pyrrolyl-beta-ketoacyl-S-PigH. In the last
CC step, PigH catalyzes the decarboxylative condensation between the
CC pyrrolyl-beta-ketoacyl (pyrrolyl-beta-ketoacyl-S-PigH) and L-serine to
CC yield 4-hydroxy-2,2'-bipyrrole-5-methanol (HBM).
CC {ECO:0000269|PubMed:15853884, ECO:0000269|PubMed:17002325}.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:17002325};
CC -!- PATHWAY: Antibiotic biosynthesis; prodigiosin biosynthesis.
CC {ECO:0000305|PubMed:15853884, ECO:0000305|PubMed:17002325}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Cells with an insertion in the ACP domain of this
CC gene show an white phenotype and produce 2-methyl-3-n-amyl-pyrrole
CC (MAP) but not prodigiosin. Cells with an insertion in the
CC aminotransferase domain of this gene show a light pink phenotype and
CC produce less prodigiosin than the wild-type.
CC {ECO:0000269|PubMed:15853884}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ833001; CAH55636.1; -; Genomic_DNA.
DR RefSeq; WP_021014646.1; NZ_CP025085.1.
DR PDB; 5Y08; NMR; -; A=1-188.
DR PDBsum; 5Y08; -.
DR AlphaFoldDB; Q5W264; -.
DR SASBDB; Q5W264; -.
DR SMR; Q5W264; -.
DR STRING; 104623.Ser39006_01376; -.
DR KEGG; ag:CAH55636; -.
DR eggNOG; COG0156; Bacteria.
DR OrthoDB; 479874at2; -.
DR UniPathway; UPA01072; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; IEA:UniProtKB-KW.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IMP:UniProtKB.
DR Gene3D; 1.10.1200.10; -; 2.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR001917; Aminotrans_II_pyridoxalP_BS.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SUPFAM; SSF47336; SSF47336; 2.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminotransferase; Antibiotic biosynthesis; Membrane;
KW Phosphopantetheine; Phosphoprotein; Pyridoxal phosphate; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..653
FT /note="4-hydroxy-2,2'-bipyrrole-5-methanol synthase PigH"
FT /id="PRO_0000436246"
FT TRANSMEM 512..532
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 7..84
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT BINDING 354..355
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P12998"
FT BINDING 379
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P12998"
FT BINDING 426
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P12998"
FT BINDING 454
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P12998"
FT BINDING 482
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P12998"
FT MOD_RES 45
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:17002325"
FT MOD_RES 485
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P12998"
FT MUTAGEN 45
FT /note="S->A: The pyrrolyl-beta-ketoacyl moiety is formed."
FT /evidence="ECO:0000269|PubMed:17002325"
FT MUTAGEN 139
FT /note="S->A: The pyrrolyl-beta-ketoacyl moiety is formed."
FT /evidence="ECO:0000269|PubMed:17002325"
FT STRAND 2..4
FT /evidence="ECO:0007829|PDB:5Y08"
FT HELIX 6..24
FT /evidence="ECO:0007829|PDB:5Y08"
FT HELIX 28..30
FT /evidence="ECO:0007829|PDB:5Y08"
FT HELIX 37..41
FT /evidence="ECO:0007829|PDB:5Y08"
FT HELIX 45..58
FT /evidence="ECO:0007829|PDB:5Y08"
FT HELIX 73..80
FT /evidence="ECO:0007829|PDB:5Y08"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:5Y08"
FT HELIX 100..118
FT /evidence="ECO:0007829|PDB:5Y08"
FT TURN 122..124
FT /evidence="ECO:0007829|PDB:5Y08"
FT TURN 131..134
FT /evidence="ECO:0007829|PDB:5Y08"
FT HELIX 139..152
FT /evidence="ECO:0007829|PDB:5Y08"
FT HELIX 167..181
FT /evidence="ECO:0007829|PDB:5Y08"
FT HELIX 185..188
FT /evidence="ECO:0007829|PDB:5Y08"
SQ SEQUENCE 653 AA; 71158 MW; EA1B50007535AC62 CRC64;
MNDVTTETYE TLKQSVLHTF AQLTGYNVSE LSLTSHLEND LGVDSIALAE IAVSLSRQFQ
LNTPLLIQDI NTIKDALDGI LQREFQLSEK VEPAAIALSG DADLWLGNLV RQIFASHSGY
DVNALALDAE IESDLGIDSV SVASAQGELF NTLQLNSETI IANCNTLSAL KQCLAARLVQ
EKGQDWFEQR GRGQSDSAID HDADTTAEVT PPTATPVAIN AEIGDPRTMR DFVGIEHPDI
FHKAREFHLF YQDKKKRQLY FYGMPLETPC KNRAVMFDEA TGQHREFLMF GSNSYLGLSN
HPEIIHAIQD AASLYGATNT GCRIIAGSNV LHLELERKLA KLKGRDDCIV YPSGYSANLG
CISALTSRHD LVFTDAINHM SIQDGCKLAG AQRKIYNHSL TSLEKSLAKY ADHPGGKLIV
TDGVFSMHGD IVDLPRLMKL AERYGARVLV DDAHSTGVLG KTGAGTSEHF NMKGQVDLEL
GTMSKALSGL GGYVCGDGDV VEYLRFYSNS YVFAATIPAP VAAGVIASID VMLREPERLA
KLWDNIYYFR TRLLNAGFDL ENSDSAIIPI VVGDDAKTLF FGRAVRARGM FCQTVVFPGV
SVGDARLRIS ITSEHTREDL DEAYAILVAS ALEVGVPVNA SAHQEENASV AEA
