ID A0A1S2VC84_9BACT Unreviewed; 998 AA.
AC A0A1S2VC84;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Amidohydrolase {ECO:0000313|EMBL:OIN56302.1};
GN ORFNames=BLX24_25675 {ECO:0000313|EMBL:OIN56302.1};
OS Arsenicibacter rosenii.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Arsenicibacter.
OX NCBI_TaxID=1750698 {ECO:0000313|EMBL:OIN56302.1, ECO:0000313|Proteomes:UP000181790};
RN [1] {ECO:0000313|EMBL:OIN56302.1, ECO:0000313|Proteomes:UP000181790}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM-1 {ECO:0000313|EMBL:OIN56302.1,
RC ECO:0000313|Proteomes:UP000181790};
RA Huang K.;
RT "Arsenicibacter rosenii gen. nov., sp. nov., an efficient arsenic-
RT methylating bacterium isolated from an arsenic-contaminated paddy soil.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TolB family.
CC {ECO:0000256|ARBA:ARBA00009820}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OIN56302.1}.
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DR EMBL; MORL01000025; OIN56302.1; -; Genomic_DNA.
DR RefSeq; WP_071506094.1; NZ_MORL01000025.1.
DR AlphaFoldDB; A0A1S2VC84; -.
DR OrthoDB; 9815657at2; -.
DR Proteomes; UP000181790; Unassembled WGS sequence.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR Gene3D; 1.20.58.520; Amidohydrolase; 1.
DR Gene3D; 3.30.110.90; Amidohydrolase; 1.
DR Gene3D; 3.40.50.10910; Amidohydrolase; 1.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 3.
DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR InterPro; IPR011659; PD40.
DR PANTHER; PTHR36842; PROTEIN TOLB HOMOLOG; 1.
DR PANTHER; PTHR36842:SF1; TOL-PAL SYSTEM PROTEIN TOLB; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR Pfam; PF07676; PD40; 7.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR SUPFAM; SSF50956; Thermostable phytase (3-phytase); 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:OIN56302.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000181790};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..998
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010346034"
FT DOMAIN 889..988
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT REGION 492..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 998 AA; 109232 MW; 4FA72D346CAA581B CRC64;
MDSNRFGWWG CLCLLFVSIS APLQATVKDS LKITVTEGTN MAIALSPDKQ TIALDLQGTI
WLVPATGGAA RPITDALGDC RQPTWSPDGR WVAFHAFWDG TYHLWMVSRD GKQKKQLTFG
IYDDREPHWS PDGKRMVFSS DRSGNYDIWQ LTVETGALTQ LTQHQANDYN PAISPDGTQI
TYVSERTETP GIYRLDPAGA ERLVAGSVAK LAAPTWSADG TQIYYNLVNK TQSGLAVTDL
AGKTQVLTPA AEDVFPFRLS WLSATEYLYT ADGRIKKQRI GQGGSVIPFS ATVTLAKRSY
ERKRYDFDQT TSLPVKGIRG PVVSPDGLKI AFAAVGDLWI LTKGNGQPKA ITNDVYLDAD
PAWSPDGQKL AFTSDRQGNM DLWVKDLQTG QEQRLVDLPD DINLPAWSPD GKRIAFYQGD
ARNVWGRGTL QIVEVSTGKV DKYHEPVFVP SQPTWSPDGK TIAVSALDVY SSRYREGISE
VLLISTDRTG DGSADRHMSP VAGRTLGTRG KNGPVWSPDG HQLAYILDGL LWTSPVDALG
NPIGPPRRLT NELADSPSWT GDSQRIVFLA TDTLKQVYLS DGHIDAIPCR FTWQIKKPSG
QVVIHAGQLF DGKSATYRKN VDIIIDGNRI KAIEPHQPNR TGRLIDASAQ TVIPGLFEMH
THQSAMCGEQ QGRLWLAYGI TSVREPGADP YDALERKEAW ASGRRKGPRQ FFTGGLTDGT
RIYYGLAIPI TSGAQLELEL NRSVRLGFDM IKTYVRMPDP IQQRITAFAH SHGLPVSSHE
IYPAMSYEVD AVEHIGGTSR RGYSPKITAM NKTYQDVIQL LAKSGMNITP TASLQGGFYV
MAGQDPGFYE NRQFKAFYPE SYLNGLQVSA AQISKINPGY ISNFGNIQAS VKALIAAGAH
VTTGTDSPFV PYGTSLHTEL QSFVGAGLSP YEALRSATLW AAETVGVSKD LGSVEPGKLA
DLVIVNGDPL TKIKDAWNVS VVLKNGEVLL IDELLKKP
//
