ARRA_CHRAT
ID ARRA_CHRAT Reviewed; 846 AA.
AC Q5Y818;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Arsenate respiratory reductase molybdopterin-containing subunit ArrA {ECO:0000305};
DE EC=1.20.99.1 {ECO:0000269|PubMed:9738904};
DE AltName: Full=Arsenate respiratory reductase large subunit {ECO:0000305};
DE Short=ARR large subunit {ECO:0000305};
DE Flags: Precursor;
GN Name=arrA {ECO:0000303|PubMed:9738904};
OS Chrysiogenes arsenatis.
OC Bacteria; Chrysiogenetes; Chrysiogenales; Chrysiogenaceae; Chrysiogenes.
OX NCBI_TaxID=309797;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 700172 / DSM 11915 / BAL-1;
RX PubMed=15486292; DOI=10.1126/science.1102374;
RA Malasarn D., Saltikov C.W., Campbell K.M., Santini J.M., Hering J.G.,
RA Newman D.K.;
RT "arrA is a reliable marker for As(V) respiration.";
RL Science 306:455-455(2004).
RN [2]
RP PROTEIN SEQUENCE OF 30-58, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, AND
RP INDUCTION.
RX PubMed=9738904; DOI=10.1046/j.1432-1327.1998.2550647.x;
RA Krafft T., Macy J.M.;
RT "Purification and characterization of the respiratory arsenate reductase of
RT Chrysiogenes arsenatis.";
RL Eur. J. Biochem. 255:647-653(1998).
CC -!- FUNCTION: Component of the arsenate respiratory reductase (Arr)
CC complex, which catalyzes the reduction of arsenate (As(V)) to arsenite
CC (As(III)) (PubMed:9738904). Can use acetate as the electron donor
CC (PubMed:9738904). ArrA is the arsenate-binding subunit (By similarity).
CC {ECO:0000250|UniProtKB:Q7WTU0, ECO:0000269|PubMed:9738904}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=A + arsenite + H2O = AH2 + arsenate + H(+);
CC Xref=Rhea:RHEA:18449, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17499, ChEBI:CHEBI:29242,
CC ChEBI:CHEBI:48597; EC=1.20.99.1;
CC Evidence={ECO:0000269|PubMed:9738904};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000305|PubMed:9738904};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250|UniProtKB:Q7WTU0};
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000269|PubMed:9738904};
CC Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-
CC bis-MGD) cofactor per subunit. {ECO:0000250|UniProtKB:Q7WTU0};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.3 mM for arsenate {ECO:0000269|PubMed:9738904};
CC Vmax=7013 umol/min/mg enzyme {ECO:0000269|PubMed:9738904};
CC -!- SUBUNIT: Heterodimer composed of one large subunit (ArrA) and one small
CC subunit (ArrB). {ECO:0000269|PubMed:9738904}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:9738904}.
CC -!- INDUCTION: Fully induced in the presence of arsenate.
CC {ECO:0000269|PubMed:9738904}.
CC -!- PTM: Predicted to be exported by the Tat system. The position of the
CC signal peptide cleavage has been experimentally proven.
CC {ECO:0000255|PROSITE-ProRule:PRU00648, ECO:0000269|PubMed:9738904}.
CC -!- MISCELLANEOUS: May also use zinc as a cofactor.
CC {ECO:0000269|PubMed:9738904}.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; AY660883; AAU11839.1; -; Genomic_DNA.
DR BioCyc; MetaCyc:MON-10841; -.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd02780; MopB_CT_Tetrathionate_Arsenate-R; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR037946; MopB_CT_Tetrathionate.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR006311; TAT_signal.
DR InterPro; IPR019546; TAT_signal_bac_arc.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SUPFAM; SSF50692; SSF50692; 1.
DR TIGRFAMs; TIGR01409; TAT_signal_seq; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS51318; TAT; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Direct protein sequencing; Iron; Iron-sulfur; Metal-binding;
KW Molybdenum; Oxidoreductase; Periplasm; Signal.
FT SIGNAL 1..29
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648,
FT ECO:0000269|PubMed:9738904"
FT CHAIN 30..846
FT /note="Arsenate respiratory reductase molybdopterin-
FT containing subunit ArrA"
FT /id="PRO_5004265100"
FT DOMAIN 43..99
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 50
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:Q7WTU0"
FT BINDING 53
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:Q7WTU0"
FT BINDING 57
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:Q7WTU0"
FT BINDING 85
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:Q7WTU0"
FT BINDING 155
FT /ligand="arsenite"
FT /ligand_id="ChEBI:CHEBI:29242"
FT /evidence="ECO:0000250|UniProtKB:Q7WTU0"
FT BINDING 156
FT /ligand="arsenate"
FT /ligand_id="ChEBI:CHEBI:48597"
FT /evidence="ECO:0000250|UniProtKB:Q7WTU0"
FT BINDING 179
FT /ligand="arsenite"
FT /ligand_id="ChEBI:CHEBI:29242"
FT /evidence="ECO:0000250|UniProtKB:Q7WTU0"
FT BINDING 180
FT /ligand="arsenate"
FT /ligand_id="ChEBI:CHEBI:48597"
FT /evidence="ECO:0000250|UniProtKB:Q7WTU0"
FT BINDING 183
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /ligand_part="Mo"
FT /ligand_part_id="ChEBI:CHEBI:28685"
FT /evidence="ECO:0000250|UniProtKB:Q7WTU0"
FT BINDING 188
FT /ligand="arsenate"
FT /ligand_id="ChEBI:CHEBI:48597"
FT /evidence="ECO:0000250|UniProtKB:Q7WTU0"
FT BINDING 200
FT /ligand="arsenite"
FT /ligand_id="ChEBI:CHEBI:29242"
FT /evidence="ECO:0000250|UniProtKB:Q7WTU0"
SQ SEQUENCE 846 AA; 94209 MW; D9BEE63288EA3B70 CRC64;
MRIKRREFLK ASAAVGAVAV ASPTLNAFAQ TGTGASAMGE AEGKWIPSTC QGCTTWCPVE
FLFRMAVRSK YAATQLSKAN NGYCCVRGHL MLQQLYDPDR IKTPMKRTNP VKGRKEDPKI
CPYHMGMKQW DTIADKIMEL RKNNETHKYL LMRGRYSDHN SIFYGDLTKM IGSPNNISHS
AICAEVEKMG SMATEGFWGY RDYDLDNMKY LIAWACDPLS SNRQIPNAIR KIQGVMDRGK
VVAVDPRMNN TASKAQEWLP IKPSEDGALA LAMAHVIITK GLWSKEFVGD FKDGKNKFVA
GKTVKEEDFE EKLTNGIVKW WNLEVKDRTP KWAAKVTGID EATIIRVATE FAQAAPACAI
WYGPNMQPRG SYAVMCIHAL NGLVGASDSE GGLCTGMGSP SSSYPKIDAY QDDVAKAGAK
NKKIDQRGTL KFPAMGSAKP GTGVVTNNVA DALLAADPYD IKVAIGYFCN FNFSGTDGAR
WDKALAKVPF FVHCVPMFSE MTYFADIVLP AALHHTEDWA VIRSKANLHG HTSIQQPVVE
RMFDVKGVET EITWLLAEKL KAKGFENMYN WLYNEYKDPE TGKNPTNSLE FALYATKIRS
KKCWDPKENA EYKGDKLNGW ADFMEKGIVN SPKFKFRQKW EKGFPTETKK FEFYSETLKK
GLLAHAEKNK VTVDQVMEAT NYEARGELAF IPHYESPKRH GDVKEFPFSL IDMKSRLNRE
GRSTNATWYH AFKKCDPGDV NQEDVLQINP ADAKKLGINE GDMVKVTSVI GSLTVKARLW
EGVRPGCVAK CYGQGHFAMG RVSAKDFGKA VARGANFNDI MPADYDRITG ATARNGGFTG
VKIEKA
