PDUS_CITFR
ID PDUS_CITFR Reviewed; 451 AA.
AC B1VB77;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Cobalamin reductase PduS {ECO:0000303|PubMed:21103360};
DE AltName: Full=Corrin reductase {ECO:0000303|PubMed:21103360};
DE AltName: Full=Propanediol utilization protein PduS;
GN Name=pduS {ECO:0000303|PubMed:18332146};
OS Citrobacter freundii.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter; Citrobacter freundii complex.
OX NCBI_TaxID=546;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
RX PubMed=18332146; DOI=10.1074/jbc.m709214200;
RA Parsons J.B., Dinesh S.D., Deery E., Leech H.K., Brindley A.A., Heldt D.,
RA Frank S., Smales C.M., Lunsdorf H., Rambach A., Gass M.H., Bleloch A.,
RA McClean K.J., Munro A.W., Rigby S.E.J., Warren M.J., Prentice M.B.;
RT "Biochemical and Structural Insights into Bacterial Organelle Form and
RT Biogenesis.";
RL J. Biol. Chem. 283:14366-14375(2008).
RN [2]
RP FUNCTION, 4FE-4S COFACTOR, FMN COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP INTERACTION WITH PDUT, AND MUTAGENESIS OF CYS-54; CYS-264; CYS-267;
RP CYS-270; CYS-274; CYS-309; CYS-312; CYS-315 AND CYS-320.
RX PubMed=21103360; DOI=10.1371/journal.pone.0014009;
RA Parsons J.B., Lawrence A.D., McLean K.J., Munro A.W., Rigby S.E.,
RA Warren M.J.;
RT "Characterisation of PduS, the pdu metabolosome corrin reductase, and
RT evidence of substructural organisation within the bacterial
RT microcompartment.";
RL PLoS ONE 5:e14009-e14009(2010).
CC -!- FUNCTION: A bifunctional cobalamin reductase that converts
CC cob(III)alamin to cob(II)alamin and then to cob(I)alamin in the
CC bacterial microcompartment (BMC) dedicated to 1,2-propanediol (1,2-PD)
CC degradation. PduS and PduO allow regeneration of the adenosylcobalamin
CC cofactor within the BMC (PubMed:21103360). Cobalamin reduction probably
CC occurs spontaneously in the presence of free reduced flavin
CC nucleotides, this protein may be involved in electron transfer for this
CC reduction (By similarity). {ECO:0000250|UniProtKB:Q9XDM9,
CC ECO:0000269|PubMed:21103360}.
CC -!- FUNCTION: Expression of a cosmid containing the full 21-gene pdu operon
CC in E.coli allows E.coli to grow on 1,2-propanediol (1,2-PD) with the
CC appearance of BMCs in its cytoplasm. {ECO:0000305}.
CC -!- FUNCTION: The 1,2-PD-specific bacterial microcompartment (BMC)
CC concentrates low levels of 1,2-PD catabolic enzymes, concentrates
CC volatile reaction intermediates thus enhancing pathway flux and keeps
CC the level of toxic, mutagenic propionaldehyde low.
CC {ECO:0000305|PubMed:18332146}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00711,
CC ECO:0000269|PubMed:21103360};
CC Note=Binds 2 [4Fe-4S] clusters (PubMed:21103360) (By similarity). The
CC two centers are coupled but must possess different redox potentials
CC (PubMed:21103360). {ECO:0000255|PROSITE-ProRule:PRU00711,
CC ECO:0000269|PubMed:21103360};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:21103360};
CC Note=Binds one FMN non-covalently per monomer.
CC {ECO:0000250|UniProtKB:Q9XDM9};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.59 mM for aquacob(III)alamin {ECO:0000269|PubMed:21103360};
CC KM=24.7 uM for NADH {ECO:0000269|PubMed:21103360};
CC Redox potential:
CC E(0) is -262 mV for aerobically purified protein (only with FMN).
CC E(0) is -150 mV for anaerobically purified protein (with FMN and 4Fe-
CC 4S centers).;
CC -!- PATHWAY: Polyol metabolism; 1,2-propanediol degradation.
CC {ECO:0000269|PubMed:18332146}.
CC -!- SUBUNIT: Monomer, forms a complex with PduO (By similarity). Interacts
CC with PduT, probably via the N-terminus of PduS (PubMed:21103360).
CC {ECO:0000250|UniProtKB:Q9XDM9, ECO:0000269|PubMed:21103360}.
CC -!- SUBCELLULAR LOCATION: Bacterial microcompartment
CC {ECO:0000250|UniProtKB:Q9XDM9}.
CC -!- SIMILARITY: Belongs to the PduS cobalamin reductase family.
CC {ECO:0000305}.
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DR EMBL; AM498294; CAM57298.1; -; Genomic_DNA.
DR UniPathway; UPA00621; -.
DR GO; GO:0031469; C:bacterial microcompartment; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051144; P:propanediol catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.1060.10; -; 1.
DR Gene3D; 3.40.50.11540; -; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR009051; Helical_ferredxn.
DR InterPro; IPR010208; Ion_transpt_RnfC/RsxC.
DR InterPro; IPR011538; Nuo51_FMN-bd.
DR InterPro; IPR037225; Nuo51_FMN-bd_sf.
DR InterPro; IPR017054; PduS.
DR InterPro; IPR026902; RnfC_N.
DR InterPro; IPR019554; Soluble_ligand-bd.
DR PANTHER; PTHR43034; PTHR43034; 2.
DR Pfam; PF01512; Complex1_51K; 1.
DR Pfam; PF13375; RnfC_N; 1.
DR Pfam; PF10531; SLBB; 1.
DR PIRSF; PIRSF036408; PduS_prd; 1.
DR SUPFAM; SSF142019; SSF142019; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 1: Evidence at protein level;
KW 4Fe-4S; Bacterial microcompartment; Electron transport; Flavoprotein; FMN;
KW Iron; Iron-sulfur; Metal-binding; NAD; Repeat; Transport.
FT CHAIN 1..451
FT /note="Cobalamin reductase PduS"
FT /id="PRO_0000454283"
FT DOMAIN 255..284
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 300..330
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 264
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 267
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 270
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 274
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 309
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 312
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 315
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 320
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT MUTAGEN 54
FT /note="C->A: Colorless protein, no 4Fe-4S centers, no
FT cobalamin reductase activity."
FT /evidence="ECO:0000269|PubMed:21103360"
FT MUTAGEN 264
FT /note="C->A: Colorless protein, no 4Fe-4S centers, no
FT cobalamin reductase activity."
FT /evidence="ECO:0000269|PubMed:21103360"
FT MUTAGEN 267
FT /note="C->A: Colorless protein, no 4Fe-4S centers, no
FT cobalamin reductase activity."
FT /evidence="ECO:0000269|PubMed:21103360"
FT MUTAGEN 270
FT /note="C->A: Colorless protein, no 4Fe-4S centers, no
FT cobalamin reductase activity."
FT /evidence="ECO:0000269|PubMed:21103360"
FT MUTAGEN 274
FT /note="C->A: Colorless protein, no 4Fe-4S centers, no
FT cobalamin reductase activity."
FT /evidence="ECO:0000269|PubMed:21103360"
FT MUTAGEN 309
FT /note="C->A: Colorless protein, no 4Fe-4S centers, no
FT cobalamin reductase activity."
FT /evidence="ECO:0000269|PubMed:21103360"
FT MUTAGEN 312
FT /note="C->A: Colorless protein, no 4Fe-4S centers, no
FT cobalamin reductase activity."
FT /evidence="ECO:0000269|PubMed:21103360"
FT MUTAGEN 315
FT /note="C->A: Colorless protein, no 4Fe-4S centers, no
FT cobalamin reductase activity."
FT /evidence="ECO:0000269|PubMed:21103360"
FT MUTAGEN 320
FT /note="C->A: Colorless protein, no 4Fe-4S centers, no
FT cobalamin reductase activity."
FT /evidence="ECO:0000269|PubMed:21103360"
SQ SEQUENCE 451 AA; 48569 MW; 873E2EF41E3DE1E6 CRC64;
MKTAMTAEST LYDAQTIRER VRAAGVVGAG GAGFPAHVKL QAQVDTFLVN AAECEPMLKV
DQQLMAVQAE RLIRGVQYAM TATGARAGII ALKEKYQRAI NALTPLLPAG IRLHILPDVY
PAGDEVLTIW MATGRRVPPA ALPVSVGVVV NNVQTVLNIT RAVEQQYPVT RRTLTVNGAV
ARPITLTVPI GMSLREVLAL AGGATVDDPG FINGGPMMGG LITSLDTPVS KTTGGLLVLP
KSHALIQRRM QDERTVLSVA KTVCEQCRLC TDLCPRHLIG HELSPHLLVR AVNYQQAATP
QLLLTALTCS ECNVCESVAC PVGISPMRIN RMLKRELRAL NHRYEGPLNP EDEMAKYRLI
PVKRLITKLG LSDWYHDAPL TETDYPTDKT TLLLRQHIGA SAIPCVLQGE HVVRGQCVAD
VPSGALGAPV HASIDGIVSE ITEQSITVIR G
