ID E1TJR4_BURSG Unreviewed; 389 AA.
AC E1TJR4;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE SubName: Full=Aralkylamine dehydrogenase {ECO:0000313|EMBL:ADN59811.1};
DE EC=1.4.9.2 {ECO:0000313|EMBL:ADN59811.1};
GN OrderedLocusNames=BC1003_3872 {ECO:0000313|EMBL:ADN59811.1};
OS Burkholderia sp. (strain CCGE1003).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=640512 {ECO:0000313|EMBL:ADN59811.1};
RN [1] {ECO:0000313|EMBL:ADN59811.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCGE1003 {ECO:0000313|EMBL:ADN59811.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Daligault H., Davenport K., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G.,
RA Martinez-Romero E., Rogel M.A., Auchtung J., Tiedje J.M., Woyke T.;
RT "Complete sequence of chromosome2 of Burkholderia sp. CCGE1003.";
RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the aromatic amine dehydrogenase heavy chain
CC family. {ECO:0000256|ARBA:ARBA00010548}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002218; ADN59811.1; -; Genomic_DNA.
DR AlphaFoldDB; E1TJR4; -.
DR STRING; 640512.BC1003_3872; -.
DR KEGG; bgf:BC1003_3872; -.
DR eggNOG; COG3391; Bacteria.
DR HOGENOM; CLU_059384_0_0_4; -.
DR OMA; WAPGGWQ; -.
DR OrthoDB; 185182at2; -.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0030058; F:amine dehydrogenase activity; IEA:InterPro.
DR GO; GO:0030059; F:aralkylamine dehydrogenase (azurin) activity; IEA:UniProtKB-EC.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR009451; Metamine_DH_Hvc.
DR InterPro; IPR011044; Quino_amine_DH_bsu.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR47197:SF3; DIHYDRO-HEME D1 DEHYDROGENASE; 1.
DR PANTHER; PTHR47197; PROTEIN NIRF; 1.
DR Pfam; PF06433; Me-amine-dh_H; 1.
DR SUPFAM; SSF50969; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR609451-50};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Oxidoreductase {ECO:0000313|EMBL:ADN59811.1};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transport {ECO:0000256|ARBA:ARBA00022982}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..389
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003152333"
FT DISULFID 184..199
FT /evidence="ECO:0000256|PIRSR:PIRSR609451-50"
SQ SEQUENCE 389 AA; 42019 MW; 9949CD486210F165 CRC64;
MERRRRAVAR AASILALSYG LLACHAQAGA AEKPEELTVA KVPPVNPHRA FVVDVSFASM
TDARVHVFDA DTSRFVGQID AGFAPGFSIS PDHKTSYVAT TYFSRGGHGT RTDVVELIDN
ATLDIVGEIE IPVKHAQAVP TPYNTTLSDD GSRLYVSNIT PSTSVTVIDT SAKKVLGEID
TDGCVLAYPS GNDRFTALCE SGKALTVKLD ATGKEVSRKL SDAFIDVEHD PAFVNAVRDG
QRYLFTTFGG RVCSADFTGD TPVFGEPWSL VTSDERKAGW RPGGLQQTAF NAINQRLYVA
MHQGSDGSHK DPATEVWVFD TVSKKRVARW KLAAQKIPPL LSIQVSADDK PLFYGLTPTS
DFVVMDAATG KLRHVDKQLG TTSTLILNP
//