ID Q2W5Q6_MAGSA Unreviewed; 911 AA.
AC Q2W5Q6;
DT 10-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 10-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE SubName: Full=Phenylacetyl CoA {ECO:0000313|EMBL:BAE50819.1};
GN OrderedLocusNames=amb2015 {ECO:0000313|EMBL:BAE50819.1};
OS Magnetospirillum magneticum (strain AMB-1 / ATCC 700264).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Magnetospirillaceae; Paramagnetospirillum.
OX NCBI_TaxID=342108 {ECO:0000313|EMBL:BAE50819.1, ECO:0000313|Proteomes:UP000007058};
RN [1] {ECO:0000313|EMBL:BAE50819.1, ECO:0000313|Proteomes:UP000007058}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AMB-1 / ATCC 700264 {ECO:0000313|Proteomes:UP000007058};
RX PubMed=16303747; DOI=10.1093/dnares/dsi002;
RA Matsunaga T., Okamura Y., Fukuda Y., Wahyudi A.T., Murase Y., Takeyama H.;
RT "Complete genome sequence of the facultative anaerobic magnetotactic
RT bacterium Magnetospirillum sp. strain AMB-1.";
RL DNA Res. 12:157-166(2005).
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR EMBL; AP007255; BAE50819.1; -; Genomic_DNA.
DR RefSeq; WP_011384418.1; NC_007626.1.
DR AlphaFoldDB; Q2W5Q6; -.
DR STRING; 342108.amb2015; -.
DR KEGG; mag:amb2015; -.
DR HOGENOM; CLU_000422_13_3_5; -.
DR OrthoDB; 9810782at2; -.
DR Proteomes; UP000007058; Chromosome.
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:InterPro.
DR CDD; cd02778; MopB_CT_Thiosulfate-R-like; 1.
DR CDD; cd02760; MopB_Phenylacetyl-CoA-OR; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.740; -; 2.
DR Gene3D; 2.20.25.90; ADC-like domains; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR041932; Phenylacetyl-CoA-OR_N.
DR PANTHER; PTHR43742:SF9; TETRATHIONATE REDUCTASE SUBUNIT A; 1.
DR PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000007058}.
FT DOMAIN 66..622
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 806..865
FT /note="Molybdopterin dinucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF01568"
SQ SEQUENCE 911 AA; 100208 MW; B71CB5662DE0A1C8 CRC64;
MSVETKSVPT YCYNCVAGPD LMCVTVKDGV AVAVTPNHAG MGIHPADGRP CVKAYGLVQK
TYNPHRVLTP MKRTNPRKGR DEDPGFVPIS WDEALDLVAG KLRSVREMGL LNEQGMPRLA
ATFGHGGTPA NYMGTFPAFL AAWGPIDFSF GSGQGVKCVH SEHLYGEYWH RAFTVAADTP
NANFIVSFGT NVEVSGGPCG VRRHADARIR GIKRVQVEPH LSPTGACSAQ WVPIRPKTDP
AFMFAMLHVM LHEAPRSALD LDFLRDRTAS PYLVDDEGWY LRDEATGKPL MWDGITGQPV
PHDHPGAVPA LEGSFTVPAA VAKLPDGEMV RRENATARTA FTLLVDGMRG YTPDWAETIC
DVPAKVVRQV ALEYLDNACV GQTTEVDGKV LPHRPVAVTL GKTVNNGWGA YECCWARTVL
ATLVGALEVP GGTLGTTVRL NRPYENRLKS VKPGEDGFMN AQMNSTKKGG WAEKPKGRNA
HTTLIPIVGD SSWAQALGPT HLAWMFLKDS PAEWAPPEPP DVWIAYRTNP AISFWDTAQL
SGNMAKMPFV VCFAYTMDET NHMADILLPE ATDLESTQLI RAGGSKFVEQ HWQHQGFVLR
QPAVAPQGES RDFTWITTEL SRRVGLLESY NRGLNKGFAL VPLKGEGFDF TLPEDQVHDV
DTIWDAVCKA ATAGATKGQE VRGLDWMKEN GFFMQPFARE DWYLHATMVE QGLRYELPYQ
ERLMRVGEEL RRRLHEAGIQ WWDEQLEEYQ GIPHWHDVPG RWVKAVERAG AKAEDFPFWG
ITTKTMPYTT GNNAGIPLMN EVAGNLRGHG SVIINASSAA KLDIKDGDWV EVSSVVGHTR
GRAALVQGCR PDTVVIPGQF QHWKTPYAKD LNFPSLNTIT QMSLELTDAT GSGADVVRVA
LRRVDGPGEP A
//
