ID A0A0Q4LXI1_9SPHI Unreviewed; 1075 AA.
AC A0A0Q4LXI1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Amidohydrolase {ECO:0000313|EMBL:KQN38661.1};
GN ORFNames=ASE92_04350 {ECO:0000313|EMBL:KQN38661.1};
OS Pedobacter sp. Leaf41.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=1736218 {ECO:0000313|EMBL:KQN38661.1, ECO:0000313|Proteomes:UP000051488};
RN [1] {ECO:0000313|Proteomes:UP000051488}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf41 {ECO:0000313|Proteomes:UP000051488};
RA Garrido-Oter R., Mueller D.B.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000051488}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf41 {ECO:0000313|Proteomes:UP000051488};
RA Vorholt J.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQN38661.1}.
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DR EMBL; LMLE01000001; KQN38661.1; -; Genomic_DNA.
DR RefSeq; WP_056848835.1; NZ_LMLE01000001.1.
DR AlphaFoldDB; A0A0Q4LXI1; -.
DR STRING; 1736218.ASE92_04350; -.
DR Proteomes; UP000051488; Unassembled WGS sequence.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 2.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 3.
DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 2.
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; 3.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF82171; DPP6 N-terminal domain-like; 2.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:KQN38661.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1075
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006226431"
FT DOMAIN 926..1027
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
SQ SEQUENCE 1075 AA; 119312 MW; 45C4BEBB68B81F7E CRC64;
MKHLYLLSAL SLLFFNITAQ EKKWDIEKYQ GTTKNFTLNT DEGTWMNLDV SADGQEIVFD
LLGDIYTMPV SGGQAKLISG GIAYDVQPRF SPNGKYISYT SDKSGGDNIW IMNRDGSGKK
QVTKESFRLL NNATWMPNGE YIVARKHFTA GRSLGAGEMW MYNINGGDGI QLTKRKNDQQ
DAGEPNVSPD GRYLYFSEDV SPGPNFEYSK DPNGTIYAIR QLDLNTGKLT TLINQQGGAC
RPQVSPDGNL IAFVKRVRLK STLYVQNIKT GEEWPVNEDL SHDQQETWAI FGVYPNFAWT
PDSKSLIFYA KGKIRKTEIA SLITSTIPFQ ANTVQTVQQA LHFEQQVYSN DFSVKMLRQL
TTSPDRKTIV FNAAGFLYKQ ELPTGTPERL TSGMDFEFEP SFSPDGKFVI YTTWSDELRG
AIKRTDIKSG KTITLSDEKG FYYSPQYSTK GDKIVFRKGS GNDVLGYNYG RGTGIFIMPA
AGGTKTLVSD NGIKPSFNNS DTRIYFQSYA DGKKALKSID LNGANERTHF TSQYANQFVV
SPDNKWLAFN ELFNVYITPM INVGTAQDAS AGNKAIPVAK VTTDGGTYMQ WSADSKNLHW
TLGPKYFTID VKNAFNFDGT TPKTQASSID INLTLKSDAP TGIVALKGAR IISMKGDEVI
ENGTILTDGN KIISIGKADA VVIPADAKVI DVNGKTIMPG IIDVHAHLRT SPDGISPQND
WSYMANLAFG VTTSHDPSSN TEMVFSQSEM LKAGRMVGPR VYSTGSILYG ADGDFKVVIN
SLDDALANLK RLKAVGAFSV KSYNQPRREQ RQQILEAARQ LKMEVLPEGG STFFHNMNMV
ADGHTGIEHS IPVLPVYKDV TTLWNNTTVG YTPTLIVAYG GQWGENYWYD RTNVWENEKL
MTYTPRSIID SRARRRTTSE YSDYNHIDIA KATKQIADGG TKVNLGAHGQ IQGLGAHWEL
WMFVQGGFSP LQAIRNATLN GAHYLGMDKE IGSLEVGKLA DLVIMDANPL DDIRNSEKIK
YVMINGRMYD SATMNEVGTR EKLRSKLWFE SAKGNGFVIP NSESETWTFT VPHCD
//