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Database: UniProt
Entry: A0A0T0PXH0_9SPHN
LinkDB: A0A0T0PXH0_9SPHN
Original site: A0A0T0PXH0_9SPHN 
ID   A0A0T0PXH0_9SPHN        Unreviewed;       411 AA.
AC   A0A0T0PXH0;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Oxidase {ECO:0000313|EMBL:KQT33737.1};
GN   ORFNames=ASG29_06950 {ECO:0000313|EMBL:KQT33737.1};
OS   Sphingomonas sp. Leaf412.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1736370 {ECO:0000313|EMBL:KQT33737.1, ECO:0000313|Proteomes:UP000051178};
RN   [1] {ECO:0000313|EMBL:KQT33737.1, ECO:0000313|Proteomes:UP000051178}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf412 {ECO:0000313|EMBL:KQT33737.1,
RC   ECO:0000313|Proteomes:UP000051178};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQT33737.1, ECO:0000313|Proteomes:UP000051178}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf412 {ECO:0000313|EMBL:KQT33737.1,
RC   ECO:0000313|Proteomes:UP000051178};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302;
CC         Evidence={ECO:0000256|ARBA:ARBA00001924};
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:KQT33737.1}.
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DR   EMBL; LMQP01000002; KQT33737.1; -; Genomic_DNA.
DR   RefSeq; WP_055982114.1; NZ_LMQP01000002.1.
DR   AlphaFoldDB; A0A0T0PXH0; -.
DR   STRING; 1736370.ASG29_06950; -.
DR   OrthoDB; 9795587at2; -.
DR   Proteomes; UP000051178; Unassembled WGS sequence.
DR   GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.650; -; 1.
DR   Gene3D; 3.90.420.10; Oxidoreductase, molybdopterin-binding domain; 1.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR005066; MoCF_OxRdtse_dimer.
DR   InterPro; IPR008335; Mopterin_OxRdtase_euk.
DR   InterPro; IPR000572; OxRdtase_Mopterin-bd_dom.
DR   InterPro; IPR036374; OxRdtase_Mopterin-bd_sf.
DR   InterPro; IPR006311; TAT_signal.
DR   PANTHER; PTHR19372:SF7; SULFITE OXIDASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR19372; SULFITE REDUCTASE; 1.
DR   Pfam; PF03404; Mo-co_dimer; 1.
DR   Pfam; PF00174; Oxidored_molyb; 1.
DR   PRINTS; PR00407; EUMOPTERIN.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   SUPFAM; SSF56524; Oxidoreductase molybdopterin-binding domain; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Molybdenum {ECO:0000256|ARBA:ARBA00022505};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051178}.
FT   DOMAIN          98..268
FT                   /note="Oxidoreductase molybdopterin-binding"
FT                   /evidence="ECO:0000259|Pfam:PF00174"
FT   DOMAIN          301..399
FT                   /note="Moybdenum cofactor oxidoreductase dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF03404"
SQ   SEQUENCE   411 AA;  44755 MW;  C37A6339E8B04108 CRC64;
     MDNFDAALAS ETSRRRFLRR TALGTAGLAA APALAQQLVD LKLPGGNAER PMTSAFPGKG
     SMILQRIHPP LLETPMDVFD KSVFTPNDQF FVRWHWADIP TSIDVESFRL KVFGHVNRPL
     SISLAQLLRL PRVEMAAVNQ CSGNSRGLFQ PRVAGAQWGN GAMGNAKWLG VRLRDVLDLA
     GVKAGAVQVR FGALDQPVVT GAPDFEKALD IDHARDGEVM IAFGMNGEQL PLLNGFPCRL
     IVPGWYSTYW VKMLNAIEVL PGPDDQYWMA KAYKIPATPG ANVAPGAKDF PTVPINRMIP
     RSWMTSLPDG QAIAYEASIP VGGIAMGGDC GVAKVDVSSD GGRTWYRTTL GADEGKYSFR
     RWDGRVPLRR GPNPIMVRCW NANGVAQPMK PIWNPGGFMR GNIETTTIIA A
//
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