ID A1THU9_MYCVP Unreviewed; 586 AA.
AC A1THU9;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE SubName: Full=UBA/THIF-type NAD/FAD binding protein {ECO:0000313|EMBL:ABM16749.1};
GN OrderedLocusNames=Mvan_5993 {ECO:0000313|EMBL:ABM16749.1};
OS Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 /
OS KCTC 9966 / NRRL B-24157 / PYR-1) (Mycobacterium vanbaalenii).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=350058 {ECO:0000313|EMBL:ABM16749.1, ECO:0000313|Proteomes:UP000009159};
RN [1] {ECO:0000313|EMBL:ABM16749.1, ECO:0000313|Proteomes:UP000009159}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 /
RC PYR-1 {ECO:0000313|Proteomes:UP000009159};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Anderson I.J., Miller C., Richardson P.;
RT "Complete sequence of Mycobacterium vanbaalenii PYR-1.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP000511; ABM16749.1; -; Genomic_DNA.
DR RefSeq; WP_011783093.1; NZ_JACKSD010000057.1.
DR AlphaFoldDB; A1THU9; -.
DR STRING; 350058.Mvan_5993; -.
DR KEGG; mva:Mvan_5993; -.
DR eggNOG; COG0476; Bacteria.
DR eggNOG; COG1310; Bacteria.
DR HOGENOM; CLU_390671_0_0_11; -.
DR Proteomes; UP000009159; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR028090; JAB_dom_prok.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR PANTHER; PTHR43267; TRNA THREONYLCARBAMOYLADENOSINE DEHYDRATASE; 1.
DR PANTHER; PTHR43267:SF1; TRNA THREONYLCARBAMOYLADENOSINE DEHYDRATASE; 1.
DR Pfam; PF14464; Prok-JAB; 1.
DR Pfam; PF00899; ThiF; 1.
DR SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
DR SUPFAM; SSF102712; JAB1/MPN domain; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000009159};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 25..117
FT /note="JAB"
FT /evidence="ECO:0000259|Pfam:PF14464"
FT DOMAIN 301..482
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
FT REGION 563..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 586 AA; 61939 MW; 0F2407C848685D88 CRC64;
MMRKQAHTAK AAEAVAGTPW SITDMVLDII DRELAVPAPE RGAALIAVRD SRLIVDVVSD
PRPGESVSYW HSDQLRRRLS DYLTDNPTRR YVGTVHSHPG GYAEPSGPDH QAFANMLATN
RAIRDAIFPI VVQAPRDGLG SVLRLGDKHL ADLPHGTFAG YSAHPTDAGL VVRPAPIHVV
PAGAHAAVVA DALTRHLGQP VTVRWGEPLT VSGTAWLTAQ FMIDTRTIAG VALGPSYPMT
PPMVWAAESA SPVFSSWPIS ATGDHLAGAV SAVLQHQTPP VAAVRAGIRE RLSVHLPNQI
DAHVLLIGAG SVGSNAAEML IRSGVKRLTV VDFDTVEPAN LSRTVYGSGD LGQLKTAALA
DRLTAIAADV EITQLTCPLQ ELTGEVLDTV DLAFLASDDM AGEGWLNHEL YVRAIPSVSV
KVFAGAEGAE LAYVLPARNT ACLRCMMGAV GSGDRGDADY GTGRINGSPA LGPDIAAAAA
RGVKVALALT QTDGPLADWL DELVSRRLTY FLSSNVAGWT YTEFARAGSL PFDGLWLTAP
GRPECEICGM ERVSDTQPAH VAAFTTSPPQ GIGDVDTDDH RHGEDN
//
