ID W0HVN3_9GAMM Unreviewed; 303 AA.
AC W0HVN3;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=Coenzyme PQQ synthesis protein B {ECO:0000256|ARBA:ARBA00015084, ECO:0000256|HAMAP-Rule:MF_00653};
DE AltName: Full=Pyrroloquinoline quinone biosynthesis protein B {ECO:0000256|ARBA:ARBA00030966, ECO:0000256|HAMAP-Rule:MF_00653};
GN Name=pqqB {ECO:0000256|HAMAP-Rule:MF_00653,
GN ECO:0000313|EMBL:AHF76567.1};
GN ORFNames=Sant_1509 {ECO:0000313|EMBL:AHF76567.1};
OS Sodalis praecaptivus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Bruguierivoracaceae; Sodalis.
OX NCBI_TaxID=1239307 {ECO:0000313|EMBL:AHF76567.1, ECO:0000313|Proteomes:UP000019028};
RN [1] {ECO:0000313|EMBL:AHF76567.1, ECO:0000313|Proteomes:UP000019028}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HS1 {ECO:0000313|EMBL:AHF76567.1,
RC ECO:0000313|Proteomes:UP000019028};
RX PubMed=24407854; DOI=10.1093/gbe/evt210;
RA Oakeson K.F., Gil R., Clayton A.L., Dunn D.M., von Niederhausern A.C.,
RA Hamil C., Aoyagi A., Duval B., Baca A., Silva F.J., Vallier A.,
RA Jackson D.G., Latorre A., Weiss R.B., Heddi A., Moya A., Dale C.;
RT "Genome degeneration and adaptation in a nascent stage of symbiosis.";
RL Genome Biol. Evol. 6:76-93(2014).
CC -!- FUNCTION: May be involved in the transport of PQQ or its precursor to
CC the periplasm. {ECO:0000256|HAMAP-Rule:MF_00653}.
CC -!- PATHWAY: Cofactor biosynthesis; pyrroloquinoline quinone biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004886, ECO:0000256|HAMAP-Rule:MF_00653}.
CC -!- SIMILARITY: Belongs to the PqqB family. {ECO:0000256|ARBA:ARBA00008481,
CC ECO:0000256|HAMAP-Rule:MF_00653}.
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DR EMBL; CP006569; AHF76567.1; -; Genomic_DNA.
DR RefSeq; WP_025421703.1; NZ_CP006569.1.
DR AlphaFoldDB; W0HVN3; -.
DR KEGG; sod:Sant_1509; -.
DR PATRIC; fig|1239307.3.peg.1642; -.
DR HOGENOM; CLU_061120_0_0_6; -.
DR OrthoDB; 9778305at2; -.
DR UniPathway; UPA00539; -.
DR Proteomes; UP000019028; Chromosome.
DR GO; GO:0018189; P:pyrroloquinoline quinone biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd16274; PQQB-like_MBL-fold; 1.
DR Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR HAMAP; MF_00653; PQQ_syn_PqqB; 1.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR011842; PQQ_synth_PqqB.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR NCBIfam; TIGR02108; PQQ_syn_pqqB; 1.
DR PANTHER; PTHR42663:SF7; COENZYME PQQ SYNTHESIS PROTEIN B; 1.
DR PANTHER; PTHR42663; HYDROLASE C777.06C-RELATED-RELATED; 1.
DR Pfam; PF12706; Lactamase_B_2; 1.
DR SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
PE 3: Inferred from homology;
KW PQQ biosynthesis {ECO:0000256|ARBA:ARBA00022905, ECO:0000256|HAMAP-
KW Rule:MF_00653}; Reference proteome {ECO:0000313|Proteomes:UP000019028};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00653}.
FT DOMAIN 51..270
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|Pfam:PF12706"
SQ SEQUENCE 303 AA; 33423 MW; D421E2992D5CCD74 CRC64;
MQIRILGTAA GGGFPQWNCN CRNCRRQRSG ELNVPSRTQS SIAVSDDGRD WVVCNVSPDI
AQQIAANPAL RNDSVLRGTA IGAIILTDSQ IDHCAGLLSL REGCPHDVWC TPEVYDDLTE
GFPVFTLLQH WNGGLRHHAL TPEQPFTVKV CPALRFTAIP LLSNAPPYSR YRDRPLPGHN
IALLVEDSRS GKRLFYAPGL GEPTPALLAW MRHADCLLLD GTLWTDDEMQ TAGVGTHRGQ
EMGHLALGGE QGLLAMFSEM PAERKIVIHI NNTNPILDDA SPERRRLMQQ GIEVSWDGMH
IEL
//
