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Database: UniProt
Entry: A0A160FU49_9BURK
LinkDB: A0A160FU49_9BURK
Original site: A0A160FU49_9BURK 
ID   A0A160FU49_9BURK        Unreviewed;      1203 AA.
AC   A0A160FU49;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Aldehyde dehydrogenase {ECO:0000313|EMBL:ANB76750.1};
GN   ORFNames=AYM40_31810 {ECO:0000313|EMBL:ANB76750.1};
OS   Paraburkholderia phytofirmans OLGA172.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=1417228 {ECO:0000313|EMBL:ANB76750.1, ECO:0000313|Proteomes:UP000076852};
RN   [1] {ECO:0000313|EMBL:ANB76750.1, ECO:0000313|Proteomes:UP000076852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OLGA172 {ECO:0000313|EMBL:ANB76750.1,
RC   ECO:0000313|Proteomes:UP000076852};
RX   PubMed=27063562; DOI=10.1016/j.gene.2016.04.018;
RA   Ricker N., Shen S.Y., Goordial J., Jin S., Fulthorpe R.R.;
RT   "PacBio SMRT assembly of a complex multi-replicon genome reveals
RT   chlorocatechol degradative operon in a region of genome plasticity.";
RL   Gene 586:239-247(2016).
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DR   EMBL; CP014579; ANB76750.1; -; Genomic_DNA.
DR   RefSeq; WP_063499962.1; NZ_CP014579.1.
DR   AlphaFoldDB; A0A160FU49; -.
DR   STRING; 1804984.AYM40_31810; -.
DR   KEGG; buz:AYM40_31810; -.
DR   Proteomes; UP000076852; Chromosome 2.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.1170.50; Aldehyde oxidase/xanthine dehydrogenase, a/b hammerhead; 1.
DR   Gene3D; 3.30.365.10; Aldehyde oxidase/xanthine dehydrogenase, molybdopterin binding domain; 4.
DR   Gene3D; 1.10.760.10; Cytochrome c-like domain; 3.
DR   InterPro; IPR000674; Ald_Oxase/Xan_DH_a/b.
DR   InterPro; IPR036856; Ald_Oxase/Xan_DH_a/b_sf.
DR   InterPro; IPR008274; AldOxase/xan_DH_MoCoBD1.
DR   InterPro; IPR046867; AldOxase/xan_DH_MoCoBD2.
DR   InterPro; IPR037165; AldOxase/xan_DH_Mopterin-bd_sf.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   PANTHER; PTHR47495; ALDEHYDE DEHYDROGENASE; 1.
DR   PANTHER; PTHR47495:SF1; BLL3820 PROTEIN; 1.
DR   Pfam; PF00034; Cytochrom_C; 2.
DR   Pfam; PF13442; Cytochrome_CBB3; 1.
DR   Pfam; PF02738; MoCoBD_1; 1.
DR   Pfam; PF20256; MoCoBD_2; 2.
DR   SMART; SM01008; Ald_Xan_dh_C; 1.
DR   SUPFAM; SSF54665; CO dehydrogenase molybdoprotein N-domain-like; 1.
DR   SUPFAM; SSF46626; Cytochrome c; 3.
DR   SUPFAM; SSF56003; Molybdenum cofactor-binding domain; 2.
DR   PROSITE; PS51007; CYTC; 3.
PE   4: Predicted;
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PROSITE-ProRule:PRU00433};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PROSITE-ProRule:PRU00433};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00433}; Reference proteome {ECO:0000313|Proteomes:UP000076852}.
FT   DOMAIN          814..917
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
FT   DOMAIN          959..1067
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
FT   DOMAIN          1091..1179
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
SQ   SEQUENCE   1203 AA;  128416 MW;  76891DD3EAA43000 CRC64;
     MTGPDLSVDR RAAPPSRRQF HDAQNVLIVT RPPQAPVRAA VGQPGSRSTF VPTEADLFLV
     VRDDGSVVAF NGHVDLGTGI GTALAQIVAE ELDVPLTRVS IVLGHTNEAP NQGPTIASAT
     IQMSAVPLRH AAAQARQFLL AEAAARLNVS AEQLDVRDGV VFQRDDAKKG IGYGELIAGR
     RIELTLSHDA PLKSPDAYKI VGKSSPRVDI PAKATGELSF VHDVRVPGML HGRVVRPPYA
     GVAQGEFIGN SLLHVDEHSI GDLPGIVKVV VIRDFVGIVA EREEVAQQAV KRLNVQWKAV
     EGLPPLETSA EVEAALRANP AKRRDLVIEG DIDAALAKDP ARTLERTYVW PFQMHASIGP
     SCAVADYRDA KLKVWSGTQN PHSLRADLAL LLALDEAHIE IVRMDAAGCY GRNCADDVAA
     DAALLSRATG SPVRVQLSRE DEHAWEPKGA AQLMDVRGAL DAEGGLAAYD FATRYPSNDA
     PTLALLLTGT ISAQPQVFEM GDRTSVPPYD YRSMRIVCDD TPPIVRASWL RGVSALPNTF
     AHESFIDELA AQAGVDPVEF RLKHLTDPRA IDLVKAVAEK AGWQPRTVAL KEAAQEDGDV
     ARGRGFAYAR YVHSKFPGFG AAWSAWIADV EVNRKSGELA VTRVVVGQDT GTMVNPDGVR
     HQIHGNVIQA TSRALKERVT FGENAVTSQE WGAYPILTFR EVPVIDVVMM PRHGEPPMGT
     GESASLPGAA AIANALYDAT GVRFRRPPFT PETIRAALAD AQAEEAAARK KKRWRLGFLG
     AIAAGAAGWL GAVAMAPQAM APIAPLRASA FAPELVARGK LLASLGNCAV CHTAHNGVPN
     AGGKALDTPF GTVYSTNITP DGQTGIGTWS LDAFVRAMRR GISRDGHRLY PVFPYTSFKN
     TSDDDLKALY AYLMAQTPVR SRPPETKLAY PFRVRPLMAA WNGLFLGRNT FAASATQSAQ
     WNRGAYLVNG LGHCSACHTP RNAFGAEKTG PAFMGGGMAE GWEAPALSTL SNAPVPWSED
     ELFSYLRYGH APLHGVAAGP MAPVVSDLTA LPDSDIRAMA TYLASLSPLE ANADPVATAR
     QYEQASTMTG TATGLGARLF DGACAVCHHT GSGPQLFGAH PSLALNTNLH STTPDNLIRV
     ILDGIGSPAR PELGTMPAYR DSFNDAQVAE LVSYLRQQFA GGKPAWQDVA ASVARIRATS
     RAE
//
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